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Conserved domains on  [gi|489507112|ref|WP_003411985|]
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MULTISPECIES: serine O-acetyltransferase [Mycobacterium]

Protein Classification

serine O-acetyltransferase( domain architecture ID 11437200)

serine O-acetyltransferase (SAT) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetyl-L-serine

CATH:  2.160.10.10
EC:  2.3.1.30
Gene Ontology:  GO:0009001|GO:0006535
PubMed:  15500694|11747907|15581568
SCOP:  4001889

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 1-171 9.52e-98

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


:

Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 281.97  E-value: 9.52e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   1 MLTAMRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFI 80
Cdd:COG1045    1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  81 DHATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVV 160
Cdd:COG1045   81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                        170
                 ....*....|.
gi 489507112 161 VGVPGQVIGQS 171
Cdd:COG1045  161 VGVPARIVKRK 171
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 1-171 9.52e-98

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 281.97  E-value: 9.52e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   1 MLTAMRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFI 80
Cdd:COG1045    1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  81 DHATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVV 160
Cdd:COG1045   81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                        170
                 ....*....|.
gi 489507112 161 VGVPGQVIGQS 171
Cdd:COG1045  161 VGVPARIVKRK 171
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 5-166 3.66e-89

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 259.92  E-value: 3.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112    5 MRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFIDHAT 84
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   85 GVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVP 164
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 489507112  165 GQ 166
Cdd:TIGR01172 161 AR 162
cysE PRK11132
serine acetyltransferase; Provisional
 1-172 1.08e-57

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 183.74  E-value: 1.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   1 MLTAMRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFI 80
Cdd:PRK11132  77 MIASAACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIML 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  81 DHATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVV 160
Cdd:PRK11132 157 DHATGIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTA 236

                        170
                 ....*....|..
gi 489507112 161 VGVPGQVIGQSQ 172
Cdd:PRK11132 237 AGVPARIVGKPE 248
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 64-164 2.28e-49

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 156.83  E-value: 2.28e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  64 TGVDIHPGAVIGARVFIDHATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSR 143
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 489507112 144 IGANAVVVKPVPPSAVVVGVP 164
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 1-35 1.56e-04

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants.and bacteria.


Pssm-ID: 198039 [Multi-domain]  Cd Length: 105  Bit Score: 39.83  E-value: 1.56e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 489507112     1 MLTAMRGDIRAARERDPAAPTALEVIFCYPGVHAV 35
Cdd:smart00971  69 IVEAAAADIQAVYDRDPACDRYLTPLLYFKGFHAL 103
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
117-146 5.17e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 5.17e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 489507112  117 HPTVGDRVIIGAGAKVLGPIKIGEDSRIGA 146
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 1-171 9.52e-98

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 281.97  E-value: 9.52e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   1 MLTAMRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFI 80
Cdd:COG1045    1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  81 DHATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVV 160
Cdd:COG1045   81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                        170
                 ....*....|.
gi 489507112 161 VGVPGQVIGQS 171
Cdd:COG1045  161 VGVPARIVKRK 171
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 5-166 3.66e-89

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 259.92  E-value: 3.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112    5 MRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFIDHAT 84
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   85 GVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVP 164
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 489507112  165 GQ 166
Cdd:TIGR01172 161 AR 162
cysE PRK11132
serine acetyltransferase; Provisional
 1-172 1.08e-57

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 183.74  E-value: 1.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   1 MLTAMRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFI 80
Cdd:PRK11132  77 MIASAACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIML 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  81 DHATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVV 160
Cdd:PRK11132 157 DHATGIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTA 236

                        170
                 ....*....|..
gi 489507112 161 VGVPGQVIGQSQ 172
Cdd:PRK11132 237 AGVPARIVGKPE 248
PLN02357 PLN02357
serine acetyltransferase
 1-169 8.91e-51

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 168.52  E-value: 8.91e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   1 MLTAMRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFI 80
Cdd:PLN02357 162 IIESVKQDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAFAVDIHPGAKIGQGILL 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  81 DHATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVV 160
Cdd:PLN02357 242 DHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTA 321


                 ....*....
gi 489507112 161 VGVPGQVIG 169
Cdd:PLN02357 322 VGNPARLIG 330
PLN02694 PLN02694
serine O-acetyltransferase
 3-192 1.48e-49

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 163.66  E-value: 1.48e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   3 TAMRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFIDH 82
Cdd:PLN02694  98 AATVADLRAARVRDPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDH 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  83 ATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVG 162
Cdd:PLN02694 178 ATGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVG 257

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489507112 163 VPGQVI-GQSQPSpggpfdwRLPDLVGASLD 192
Cdd:PLN02694 258 NPARLVgGKEKPA-------KHEECPGESMD 281
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 64-164 2.28e-49

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 156.83  E-value: 2.28e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  64 TGVDIHPGAVIGARVFIDHATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSR 143
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 489507112 144 IGANAVVVKPVPPSAVVVGVP 164
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
PLN02739 PLN02739
serine acetyltransferase
 3-174 1.14e-45

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 155.19  E-value: 1.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   3 TAMRGDIRAARERDPAAPTALEVIFCYPGVHAVWGHRLAHWLWQRGARLLARAAAEFTRILTGVDIHPGAVIGARVFIDH 82
Cdd:PLN02739 143 SSIRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDH 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  83 ATGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVG 162
Cdd:PLN02739 223 GTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAG 302

                        170
                 ....*....|....*
gi 489507112 163 VPGQVIG---QSQPS 174
Cdd:PLN02739 303 NPAKLIGfvdEQDPS 317
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 65-164 2.71e-20

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 84.84  E-value: 2.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  65 GVDIHPGAVIGARVFI-DHA---TGVVIGETAEVGDDVTIYHGVTLGGsgmvggkrHPTVGDRVIIGAGAKVLGPIKIGE 140
Cdd:cd03360  102 GCVIMAGAVINPDARIgDNViinTGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAFIGAGATIIQGVTIGA 173

                         90       100
                 ....*....|....*....|....
gi 489507112 141 DSRIGANAVVVKPVPPSAVVVGVP 164
Cdd:cd03360  174 GAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 62-164 1.01e-19

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 83.31  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   62 ILTGVDIHPGAVIGARVFIDhaTGVVIGETAEVGDDVTIYHGVTLGGsgmvggkrHPTVGDRVIIGAGAKVLGPIKIGED 141
Cdd:TIGR03570 108 IMAGAVINPDVRIGDNVIIN--TGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVFIGAGATIIQGVTIGAG 177

                          90       100
                  ....*....|....*....|...
gi 489507112  142 SRIGANAVVVKPVPPSAVVVGVP 164
Cdd:TIGR03570 178 AIVGAGAVVTKDIPDGGVVVGVP 200
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
58-170 3.69e-19

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 80.30  E-value: 3.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  58 EFTRILTGVDIHPG-AVIGARVFIDHATGVVIGETAEVGDDVTIYHGVTLGGSG--------MVGGKRHPTVGDRVIIGA 128
Cdd:COG0110   13 DGVVIGPGVRIYGGnITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNhpiddpatFPLRTGPVTIGDDVWIGA 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489507112 129 GAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVIGQ 170
Cdd:COG0110   93 GATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 60-169 4.62e-19

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 79.47  E-value: 4.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  60 TRILTGVDIHPGAVIGARVFIDhaTGVVIGETAEVGDDVTIYHGVTL------GGSGMVGGK-RHPTVGDRVIIGAGAKV 132
Cdd:cd03358    5 CIIGTNVFIENDVKIGDNVKIQ--SNVSIYEGVTIEDDVFIGPNVVFtndlypRSKIYRKWElKGTTVKRGASIGANATI 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489507112 133 LGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVIG 169
Cdd:cd03358   83 LPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK10191 PRK10191
putative acyl transferase; Provisional
 59-167 3.18e-17

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 75.31  E-value: 3.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  59 FTRILTGVDIHPGAVIGARVFIDHATGVVIGETAEVGDDVTIYHGVTLGGSGmVGGKRHPTVGDRVIIGAGAKVLGPIKI 138
Cdd:PRK10191  35 ITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRG-ADNMACPHIGNGVELGANVIILGDITI 113

                         90       100
                 ....*....|....*....|....*....
gi 489507112 139 GEDSRIGANAVVVKPVPPSAVVVGVPGQV 167
Cdd:PRK10191 114 GNNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 65-168 3.84e-16

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 71.33  E-value: 3.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  65 GVDIHPGAVIGARVFIDHATGVVIGETAEVGDDVTIY---HGVT-LGGSGMVGGKRHPTV-GDRVIIGAGAKVLGPIKIG 139
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYdhnHDIDdPERPIEQGVTSAPIViGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 489507112 140 EDSRIGANAVVVKPVPPSAVVVGVPGQVI 168
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 72-150 9.99e-14

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 64.19  E-value: 9.99e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489507112  72 AVIGARVFIDHatGVVIGETAEVGDDVTIYHGVTLGGSGMVGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVV 150
Cdd:cd00208    1 VFIGEGVKIHP--KAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 65-168 1.11e-13

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 66.29  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  65 GVDIHpgavIGARVFIDHatGVVIGETAEV--GDDVTIYHGVTLGGSGmvggkrHP----------------TVGDRVII 126
Cdd:cd03357   60 GYNIH----IGDNFYANF--NCTILDVAPVtiGDNVLIGPNVQIYTAG------HPldpeernrgleyakpiTIGDNVWI 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489507112 127 GAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVI 168
Cdd:cd03357  128 GGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 65-170 3.16e-12

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 62.35  E-value: 3.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  65 GVDIHPGAVI---GARVFIDHAT----GVVI----GETAEVGDDVTIYHGVTLGGSgmvggkrhpTVGDRVIIGAGAKVL 133
Cdd:COG0663   34 DVSVWPGAVLrgdVGPIRIGEGSniqdGVVLhvdpGYPLTIGDDVTIGHGAILHGC---------TIGDNVLIGMGAIVL 104

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489507112 134 GPIKIGEDSRIGANAVVV--KPVPPSAVVVGVPGQVIGQ 170
Cdd:COG0663  105 DGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRE 143
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 73-170 2.44e-11

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 59.73  E-value: 2.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  73 VIGARVFI-DHAT-GVVIGETAEVGDDVTIYHGVTLGGSgmvggkrhpTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVV 150
Cdd:cd04645   40 RIGERTNIqDGSVlHVDPGYPTIIGDNVTVGHGAVLHGC---------TIGDNCLIGMGAIILDGAVIGKGSIVAAGSLV 110

                         90       100
                 ....*....|....*....|..
gi 489507112 151 V--KPVPPSAVVVGVPGQVIGQ 170
Cdd:cd04645  111 PpgKVIPPGSLVAGSPAKVVRE 132
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 115-170 4.00e-11

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 59.09  E-value: 4.00e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489507112 115 KRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVIGQ 170
Cdd:cd03349   71 KGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 61-170 4.31e-11

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 59.12  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  61 RILTGVDIHPGAVIGARVFIDHATGV-------------VIGETAEVGDDVTIY--HG--------VTLGGSGMVGGKRh 117
Cdd:cd04650    2 RISPKAYVHPTSYVIGDVVIGELTSVwhyavirgdndsiYIGKYSNVQENVSIHtdHGypteigdyVTIGHNAVVHGAK- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489507112 118 ptVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVV--KPVPPSAVVVGVPGQVIGQ 170
Cdd:cd04650   81 --VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRK 133
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 65-150 4.08e-10

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 58.49  E-value: 4.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  65 GVDIHPGAVIGARVFI-DHAT---GVVIGETAEVGDDVTIYHGVTLGgsgmvggkRHPTVGDRVIIGAGA---------- 130
Cdd:COG1044  114 GVSIGPFAVIGAGVVIgDGVVigpGVVIGDGVVIGDDCVLHPNVTIY--------ERCVIGDRVIIHSGAvigadgfgfa 185

                         90       100       110
                 ....*....|....*....|....*....|
gi 489507112 131 --------KV--LGPIKIGEDSRIGANAVV 150
Cdd:COG1044  186 pdedggwvKIpqLGRVVIGDDVEIGANTTI 215
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 67-170 7.09e-10

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 57.84  E-value: 7.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  67 DIHPGAVIGarvfidhatgvvigETAEVGDDVTIYHGVTLGgsgmvggkRHPTVGDRVIIGAGAkVLGP-IKIGEDSRIG 145
Cdd:PRK00892 102 GIHPSAVID--------------PSAKIGEGVSIGPNAVIG--------AGVVIGDGVVIGAGA-VIGDgVKIGADCRLH 158

                         90       100       110
                 ....*....|....*....|....*....|
gi 489507112 146 ANAVVVkpvppSAVVVG-----VPGQVIGQ 170
Cdd:PRK00892 159 ANVTIY-----HAVRIGnrviiHSGAVIGS 183
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 58-166 1.25e-09

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 55.88  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  58 EFTRILTGVDIHPGAVIGARVF-----------IDHATGVVIGETAEVG----------DD------------VTIYHGV 104
Cdd:cd03352   54 EGCIIGDRVIIHSGAVIGSDGFgfapdgggwvkIPQLGGVIIGDDVEIGanttidrgalGDtvigdgtkidnlVQIAHNV 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489507112 105 TLG-------GSGMVGGKrhpTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQ 166
Cdd:cd03352  134 RIGencliaaQVGIAGST---TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 65-168 1.42e-09

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 55.78  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  65 GVDIHpgavIGARVFIDHATGVVIGETAEVGDDVTIYHGVTLGGSGmvggkrHP----------------TVGDRVIIGA 128
Cdd:PRK09527  73 GSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTG------HPvhhelrkngemysfpiTIGNNVWIGS 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489507112 129 GAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVI 168
Cdd:PRK09527 143 HVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI 182
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 68-166 1.65e-09

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 56.56  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  68 IHPGAVIGARVF------------IDHATGVVIGETAEVG----------DD------------VTIYHGVTLG------ 107
Cdd:COG1044  171 IHSGAVIGADGFgfapdedggwvkIPQLGRVVIGDDVEIGanttidrgalGDtvigdgtkidnlVQIAHNVRIGehtaia 250

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112 108 -GSGMVGGKrhpTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQ 166
Cdd:COG1044  251 aQVGIAGST---KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 58-164 4.58e-09

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273834 [Multi-domain]  Cd Length: 324  Bit Score: 55.37  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   58 EFTRILTGVDIHPGAVIGARVF------------IDHATGVVIGETAEVG----------DD------------VTIYHG 103
Cdd:TIGR01853 156 ERVQLGKNVIIHSGAVIGSDGFgyahtangghvkIPQIGRVIIEDDVEIGanttidrgafDDtiigegtkidnlVQIAHN 235

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489507112  104 VTLG-------GSGMVGGKrhpTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVP 164
Cdd:TIGR01853 236 CRIGenciivaQVGIAGST---KIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGVYGGIP 300
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 65-150 5.62e-09

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 53.95  E-value: 5.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  65 GVDIHPGAVIGARVFI-DHAT---GVVIGETAEVGDDVTIYHGVTLGgsgmvggkRHPTVGDRVIIGAGAKV-------- 132
Cdd:cd03352    7 NVSIGPNAVIGEGVVIgDGVVigpGVVIGDGVVIGDDCVIHPNVTIY--------EGCIIGDRVIIHSGAVIgsdgfgfa 78

                         90       100
                 ....*....|....*....|....*....
gi 489507112 133 -----------LGPIKIGEDSRIGANAVV 150
Cdd:cd03352   79 pdgggwvkipqLGGVIIGDDVEIGANTTI 107
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 68-150 1.19e-08

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 54.25  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  68 IHPGAVIGarvfidhatgvvigETAEVGDDVTIYHGVTLGgsgmvggkRHPTVGDRVIIGAGAkVLGP-IKIGEDSRIGA 146
Cdd:COG1044   99 IHPSAVID--------------PSAKIGEGVSIGPFAVIG--------AGVVIGDGVVIGPGV-VIGDgVVIGDDCVLHP 155


                 ....
gi 489507112 147 NAVV 150
Cdd:COG1044  156 NVTI 159
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 72-168 1.91e-08

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 53.78  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  72 AVIGARVFIDHATgvVIGEtAEVGDDVTIyhgvtlgGSGMV-----GGKRHPTV-GDRVIIGAGAKVLGPIKIGEDSRIG 145
Cdd:PRK14360 349 SQLGEGSKVNHLS--YIGD-ATLGEQVNI-------GAGTItanydGVKKHRTViGDRSKTGANSVLVAPITLGEDVTVA 418

                         90       100
                 ....*....|....*....|...
gi 489507112 146 ANAVVVKPVPPSAVVVGVPGQVI 168
Cdd:PRK14360 419 AGSTITKDVPDNSLAIARSRQVI 441
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 60-162 2.35e-08

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.22  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  60 TRILTGVDIHPGAVIGARVF-----------IDHATGVVIGETAEVG----------DD------------VTIYHGVTL 106
Cdd:PRK00892 167 VRIGNRVIIHSGAVIGSDGFgfandrggwvkIPQLGRVIIGDDVEIGanttidrgalDDtvigegvkidnlVQIAHNVVI 246

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489507112 107 G-------GSGMVGGKrhpTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVG 162
Cdd:PRK00892 247 GrhtaiaaQVGIAGST---KIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSS 306
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 72-150 3.74e-08

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 51.64  E-value: 3.74e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489507112  72 AVIGARVFIDHatGVVIGETAEVGDDVTIYHGVTLGgsgmvggkRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVV 150
Cdd:cd03352    2 AKIGENVSIGP--NAVIGEGVVIGDGVVIGPGVVIG--------DGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 94-169 5.14e-08

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 52.05  E-value: 5.14e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489507112  94 VGDDVTIYHGVTLGGsgmvggkrHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVIG 169
Cdd:cd03351  123 IGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 59-166 1.78e-07

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 49.73  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  59 FTRILTGVDIHPGAVIGARVFIDHATgvvIGET-----------AEVGDDVTIyhgvtlgGSGMV-----GGKRHPTV-G 121
Cdd:cd03353   79 FAHLRPGTVLGEGVHIGNFVEIKKST---IGEGskanhlsylgdAEIGEGVNI-------GAGTItcnydGVNKHRTViG 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489507112 122 DRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQ 166
Cdd:cd03353  149 DNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIARARQ 193
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 65-169 2.66e-07

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 50.02  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  65 GVDIHPGAV-------IGARVFIdhATGVVIGETAEVGDDVTIYHGVTLGGsgmvggkrHPTVGDRVIIGAGAKVLGPIK 137
Cdd:COG1043   91 FVTIHRGTVqgggvtrIGDDNLL--MAYVHVAHDCVVGNNVILANNATLAG--------HVEVGDHAIIGGLSAVHQFVR 160

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489507112 138 IGEDSRIGANAVVVKPVPPSAVVVGVPGQVIG 169
Cdd:COG1043  161 IGAHAMVGGGSGVVKDVPPYVLAAGNPARLRG 192
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 59-168 2.91e-07

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 50.15  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  59 FTRILTGVDIHPGAVIGARVFIDHATgvvIGET-----------AEVGDDVTIyhgvtlgGSGMV-----GGKRHPT-VG 121
Cdd:PRK14357 318 FSRLREGTVLKKSVKIGNFVEIKKST---IGENtkaqhltylgdATVGKNVNI-------GAGTItcnydGKKKNPTfIE 387

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489507112 122 DRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVI 168
Cdd:PRK14357 388 DGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIV 434
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
60-169 3.22e-07

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 49.71  E-value: 3.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  60 TRILTGVDIHPGAVIGA------------RVFI-DHAT---GVVI--------GET-----------------AEVGDDV 98
Cdd:PRK05289  51 TTIGKNNRIFPFASIGEdpqdlkykgeptRLVIgDNNTireFVTInrgtvqggGVTrigdnnllmayvhvahdCVVGNHV 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489507112  99 TIYHGVTLGGsgmvggkrHPTVGDRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVIG 169
Cdd:PRK05289 131 ILANNATLAG--------HVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRG 193
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
68-150 5.21e-07

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 48.94  E-value: 5.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  68 IHPGAVIGArvfidhatGVVIGETAEVGDDVTIyhgvtlggsgmvggkrhptvGDRVIIGAGAKVLGPIKIGEDSRIGAN 147
Cdd:PRK05289  11 VEPGAKIGE--------NVEIGPFCVIGPNVVI--------------------GDGTVIGSHVVIDGHTTIGKNNRIFPF 62


                 ...
gi 489507112 148 AVV 150
Cdd:PRK05289  63 ASI 65
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 58-169 7.89e-07

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 48.41  E-value: 7.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   58 EFTRILTGVDIHPGAV--IGARVFIDHA---TGVVIGETAEVGDDVTIYHGVTLGGsgmvggkrHPTVGDRVIIGAGAKV 132
Cdd:TIGR01852  81 DNNTIREFVTINRGTAsgGGVTRIGNNNllmAYSHIAHDCVVGNHVILANNATLAG--------HVEVGDYAIIGGLVAV 152

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489507112  133 LGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVIG 169
Cdd:TIGR01852 153 HQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARLRG 189
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 68-168 1.37e-06

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 48.10  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  68 IHPGAVIGARVFIdhatG-------VVIGE-----------TAEVGDDVTIyhgvtlgGSGMV-----GGKRHPTV-GDR 123
Cdd:COG1207  332 LRPGTVLGEGVKI----GnfvevknSTIGEgskvnhlsyigDAEIGEGVNI-------GAGTItcnydGVNKHRTViGDG 400

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489507112 124 VIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVI 168
Cdd:COG1207  401 AFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIARARQRN 445
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 68-150 1.51e-06

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 47.43  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  68 IHPGAVIGArvfidhatGVVIGETAEVGDDVTIyhgvtlggsgmvggkrhptvGDRVIIGAGAKVLGPIKIGEDSRIGAN 147
Cdd:cd03351    8 VDPGAKIGE--------NVEIGPFCVIGPNVEI--------------------GDGTVIGSHVVIDGPTTIGKNNRIFPF 59


                 ...
gi 489507112 148 AVV 150
Cdd:cd03351   60 ASI 62
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 90-168 2.53e-06

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 46.41  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  90 ETAEVGDDVTIY---------HGVTLGGSGMVGGKRHPT----------VGDRVIIGAGAKVLGPIKIGEDSRIGANAVV 150
Cdd:PRK09677  84 ESITIGRDTLIAskvfitdhnHGSFKHSDDFSSPNLPPDmrtlessavvIGQRVWIGENVTILPGVSIGNGCIVGANSVV 163

                         90
                 ....*....|....*...
gi 489507112 151 VKPVPPSAVVVGVPGQVI 168
Cdd:PRK09677 164 TKSIPENTVIAGNPAKII 181
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 68-150 3.22e-06

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 46.55  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  68 IHPGAVIGArvfidhatGVVIGETAEVGDDVTIyhgvtlggsgmvggkrhptvGDRVIIGAGAKVLGPIKIGEDSRIGAN 147
Cdd:COG1043   10 VDPGAKLGE--------NVEIGPFCVIGPDVEI--------------------GDGTVIGSHVVIEGPTTIGKNNRIFPF 61


                 ...
gi 489507112 148 AVV 150
Cdd:COG1043   62 ASI 64
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 68-150 1.14e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 45.01  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  68 IHPGAVIGARVFIdhATGVVIGETAEVGDDVTIyhgvtlggsgmvggkrhptvGDRVIIGAGAKVLGPIKIGEDSRIGAN 147
Cdd:PRK12461   2 IHPTAVIDPSAKL--GSGVEIGPFAVIGANVEI--------------------GDGTWIGPHAVILGPTRIGKNNKIHQG 59


                 ...
gi 489507112 148 AVV 150
Cdd:PRK12461  60 AVV 62
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 119-170 1.74e-05

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 44.03  E-value: 1.74e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489507112 119 TVGDRVIIGaGAKVLGP-IKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVIGQ 170
Cdd:PRK10092 131 TIGNNVWIG-GRAVINPgVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKK 182
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 71-162 2.08e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 44.82  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  71 GAVIGARVFIDHATgvVIGEtAEVGDDVTIyhgvtlgGSGMV-----GGKRHPT-VGDRVIIGAGAKVLGPIKIGEDSRI 144
Cdd:PRK14354 351 KSTIGEGTKVSHLT--YIGD-AEVGENVNI-------GCGTItvnydGKNKFKTiIGDNAFIGCNSNLVAPVTVGDNAYI 420

                         90
                 ....*....|....*...
gi 489507112 145 GANAVVVKPVPPSAVVVG 162
Cdd:PRK14354 421 AAGSTITKDVPEDALAIA 438
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 61-163 3.98e-05

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 42.61  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  61 RILTGVDIHPGAVIGArvfiDHATGVVIGETAEVGDDVTIyHGvtLGGSGMvggkrhpTVGDRVIIGAGAKVLGPIKIGE 140
Cdd:cd00710   22 IIGDNVFVGPGASIRA----DEGTPIIIGANVNIQDGVVI-HA--LEGYSV-------WIGKNVSIAHGAIVHGPAYIGD 87

                         90       100       110
                 ....*....|....*....|....*....|
gi 489507112 141 DSRIGANAVVVKP-------VPPSAVVVGV 163
Cdd:cd00710   88 NCFIGFRSVVFNAkvgdncvIGHNAVVDGV 117
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 72-168 8.51e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 42.79  E-value: 8.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  72 AVIGARVFIDHATgvVIGEtAEVGDDVTIyhgvtlgGSGMV-----GGKRHPTV-GDRVIIGAGAKVLGPIKIGEDSRIG 145
Cdd:PRK14356 357 AVLGKGAKANHLT--YLGD-AEIGAGANI-------GAGTItcnydGVNKHRTViGEGAFIGSNTALVAPVTIGDGALVG 426

                         90       100
                 ....*....|....*....|...
gi 489507112 146 ANAVVVKPVPPSAVVVGVPGQVI 168
Cdd:PRK14356 427 AGSVITKDVPDGSLAIARGRQKN 449
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 68-146 8.70e-05

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 39.92  E-value: 8.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  68 IHPGAVIGARVFIDHatgVVIGETAEVGDDVTIYHGVTLGGSgMVGGK---RHPTVGDRVIIGAGAKVLGPIKIGEDSRI 144
Cdd:cd03356    2 IGESTVIGENAIIKN---SVIGDNVRIGDGVTITNSILMDNV-TIGANsviVDSIIGDNAVIGENVRVVNLCIIGDDVVV 77


                 ..
gi 489507112 145 GA 146
Cdd:cd03356   78 ED 79
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 79-151 8.71e-05

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 42.71  E-value: 8.71e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489507112  79 FIDHATgVVIGETAEVGDDVTIYHGVTLGGsgmvggkrHPTVGDRVIIGAGAkVLgpikigEDSRIGANAVVV 151
Cdd:COG1207  255 IIDPAT-TYIDGDVEIGRDVVIDPNVILEG--------KTVIGEGVVIGPNC-TL------KDSTIGDGVVIK 311
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 70-167 1.02e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.81  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  70 PGAVIGARVFIDH---ATGVVIGE-----------TAEVGDDVTIyhgvtlgGSGMV-----GGKRHPTV-GDRVIIGAG 129
Cdd:PRK14355 337 PGTELSAHVKIGNfveTKKIVMGEgskashltylgDATIGRNVNI-------GCGTItcnydGVKKHRTViEDDVFVGSD 409

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489507112 130 AKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQV 167
Cdd:PRK14355 410 VQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAIARSPQV 447
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 62-161 1.03e-04

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 40.83  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  62 ILTGVDIHPGAVIGARVFIDhaTGVVIGETAEVGDdvtiyhGVTLGGSGMVGGKRHP------TVGDRVIIGAGAKVLGP 135
Cdd:cd03350   22 LMMPSYVNIGAYVDEGTMVD--SWATVGSCAQIGK------NVHLSAGAVIGGVLEPlqatpvIIEDDVFIGANCEVVEG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489507112 136 IKIGEDSRIGANAVVVK---------------PVPPSAVVV 161
Cdd:cd03350   94 VIVGKGAVLAAGVVLTQstpiydretgeiyygRVPPGSVVV 134
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 74-168 1.17e-04

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 40.28  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  74 IGARVFIDHATGVVIGetaevgDDVTIYHGVTL-GGSGMVGGKRHP------TVGDRVIIGAGAKVLGPIKIGEDSRIGA 146
Cdd:cd05825   12 IGEGVWIYNLAPVTIG------SDACISQGAYLcTGSHDYRSPAFPlitapiVIGDGAWVAAEAFVGPGVTIGEGAVVGA 85

                         90       100
                 ....*....|....*....|..
gi 489507112 147 NAVVVKPVPPSAVVVGVPGQVI 168
Cdd:cd05825   86 RSVVVRDLPAWTVYAGNPAVPV 107
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 1-35 1.56e-04

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants.and bacteria.


Pssm-ID: 198039 [Multi-domain]  Cd Length: 105  Bit Score: 39.83  E-value: 1.56e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 489507112     1 MLTAMRGDIRAARERDPAAPTALEVIFCYPGVHAV 35
Cdd:smart00971  69 IVEAAAADIQAVYDRDPACDRYLTPLLYFKGFHAL 103
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 79-150 2.13e-04

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 40.87  E-value: 2.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489507112  79 FIDHATgVVIGETAEVGDDVTIYHGVTLGGsgmvggkrHPTVGDRVIIGAGAkVLGPIKIGEDSRIGANAVV 150
Cdd:cd03353    4 LIDPET-TYIDGDVEIGVDVVIDPGVILEG--------KTVIGEDCVIGPNC-VIKDSTIGDGVVIKASSVI 65
PRK10502 PRK10502
putative acyl transferase; Provisional
 63-170 2.30e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 40.70  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  63 LTGVDIHPGAVIGARVFIDHATGVVIGETAEVGDDVTIYH--GVTLG-------GSGMVGGKRHP------------TVG 121
Cdd:PRK10502  49 LFGAKIGKGVVIRPSVRITYPWKLTIGDYAWIGDDVWLYNlgEITIGahcvisqKSYLCTGSHDYsdphfdlntapiVIG 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489507112 122 DRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVVGVPGQVIGQ 170
Cdd:PRK10502 129 EGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 79-150 2.31e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.74  E-value: 2.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489507112  79 FIDHATgVVIGETAEVGDDVTIYHGVTLGGsgmvggkrHPTVGDRVIIGAGAKVlgpikigEDSRIGANAVV 150
Cdd:PRK14354 254 IIDPES-TYIDADVEIGSDTVIEPGVVIKG--------NTVIGEDCVIGPGSRI-------VDSTIGDGVTI 309
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 60-152 4.61e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 40.68  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  60 TRILTGVDIHPGAVIgarvfidhatgvvigETAEVGDDVTIYHGVTlggsgmvggkRHPTVGDRVIIGAGAKVLGPIKIG 139
Cdd:PRK14360 281 TVIGSGCRIGPGSLI---------------ENSQIGENVTVLYSVV----------SDSQIGDGVKIGPYAHLRPEAQIG 335

                         90
                 ....*....|...
gi 489507112 140 EDSRIGaNAVVVK 152
Cdd:PRK14360 336 SNCRIG-NFVEIK 347
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 72-161 5.04e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 40.69  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  72 AVIGARVFIDHATGV---VIGETAEVG-DDVTI-YHGVTlggsgmvggKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIGA 146
Cdd:PRK14352 358 ATIGRGTKVPHLTYVgdaDIGEHSNIGaSSVFVnYDGVN---------KHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGA 428

                         90
                 ....*....|....*
gi 489507112 147 NAVVVKPVPPSAVVV 161
Cdd:PRK14352 429 GTVIREDVPPGALAV 443
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
117-146 5.17e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 5.17e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 489507112  117 HPTVGDRVIIGAGAKVLGPIKIGEDSRIGA 146
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 72-168 8.15e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 39.85  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  72 AVIGARVFIDHATGV---VIGETAEVGDDvTI---YHGVtlggsgmvgGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIG 145
Cdd:PRK14353 339 AKLGEGAKVNHLTYIgdaTIGAGANIGAG-TItcnYDGF---------NKHRTEIGAGAFIGSNSALVAPVTIGDGAYIA 408

                         90       100
                 ....*....|....*....|...
gi 489507112 146 ANAVVVKPVPPSAVVVGVPGQVI 168
Cdd:PRK14353 409 SGSVITEDVPDDALALGRARQET 431
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 71-164 1.65e-03

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 38.96  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112   71 GAVIGARVFIDhatGVVIGET--AEVGDDVTIYHGVTLGGSGM---VGGKRHPTVGDRVIIGAGAKVLGPIKIGEDSRIG 145
Cdd:TIGR02353 597 GVKIGRGVYID---GTDLTERdlVTIGDDSTLNEGSVIQTHLFedrVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLG 673

                          90       100
                  ....*....|....*....|.
gi 489507112  146 ANAVVVK--PVPPSAVVVGVP 164
Cdd:TIGR02353 674 PDSLVMKgeEVPAHTRWRGNP 694
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 61-113 1.86e-03

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 36.07  E-value: 1.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489507112  61 RILTGVDIHPGAVIGARVFIDHATGVVIGETAEVGDDVTIYHGVTLGGSGMVG 113
Cdd:cd00208   20 VIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIG 72
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 60-150 2.36e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.08  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  60 TRILTGVDIHPGAVIGA----RVFIDHATGVVIGETAEVGDDVTIYHGVTLGGSGMVG------GKRH----PTVGDRVI 125
Cdd:PRK12461  48 TRIGKNNKIHQGAVVGDepqdFTYKGEESRLEIGDRNVIREGVTIHRGTKGGGVTRIGndnllmAYSHvahdCQIGNNVI 127

                         90       100
                 ....*....|....*....|....*
gi 489507112 126 IGAGAKVLGPIKIGEDSRIGANAVV 150
Cdd:PRK12461 128 LVNGALLAGHVTVGDRAIISGNCLV 152
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 68-168 2.60e-03

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 37.35  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  68 IHPGAV------IGARVFID-HAT------GVVIGETAEVGDDVTIyHG-----VTLGGSGMVGgkrHP------TVGDR 123
Cdd:cd04745    9 VHPTAVligdviIGKNCYIGpHASlrgdfgRIVIRDGANVQDNCVI-HGfpgqdTVLEENGHIG---HGailhgcTIGRN 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489507112 124 VIIGAGAKVLGPIKIGEDSRIGANAVVVK--PVPPSAVVVGVPGQVI 168
Cdd:cd04745   85 ALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVI 131
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 59-161 2.76e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.47  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  59 FTRILTGVDIHPGAVIGARVFIDHATgvvIGE-----------TAEVGDDVTIyhgvtlgGSGMV-----GGKRHPTV-G 121
Cdd:PRK09451 329 FARLRPGAELAEGAHVGNFVEMKKAR---LGKgskaghltylgDAEIGDNVNI-------GAGTItcnydGANKFKTIiG 398

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489507112 122 DRVIIGAGAKVLGPIKIGEDSRIGANAVVVKPVPPSAVVV 161
Cdd:PRK09451 399 DDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVI 438
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 1-34 3.44e-03

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants and bacteria.


Pssm-ID: 461909 [Multi-domain]  Cd Length: 104  Bit Score: 35.90  E-value: 3.44e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 489507112    1 MLTAMRGDIRAARERDPAAPTALEVIFCYPGVHA 34
Cdd:pfam06426  69 IVEAARADLQAVYERDPACDRYLTPLLYFKGFHA 102
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 87-169 4.96e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 34.91  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489507112  87 VIGETAEVGDDVTIYHGVtlggsgmvggkrhptVGDRVIIGAGAKVLGPIkIGEDSRIGANAVVVKPVPPSAVVVG---- 162
Cdd:cd03356    1 LIGESTVIGENAIIKNSV---------------IGDNVRIGDGVTITNSI-LMDNVTIGANSVIVDSIIGDNAVIGenvr 64


                 ....*...
gi 489507112 163 -VPGQVIG 169
Cdd:cd03356   65 vVNLCIIG 72
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 68-100 9.03e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 36.77  E-value: 9.03e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 489507112  68 IHPGAVIGARVFIDHAtgvVIGETAEVGDDVTI 100
Cdd:PRK05293 328 IMPGAKIGENVVIERA---IIGENAVIGDGVII 357
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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