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Conserved domains on  [gi|1148544270|ref|WP_077292168|]
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aminotransferase class V-fold PLP-dependent enzyme [Roseibium algicola]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 13-379 1.88e-118

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member PRK11706:

Pssm-ID: 450240  Cd Length: 375  Bit Score: 348.36  E-value: 1.88e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  13 IRFHAPHIPPATYDAVASALSSKHLRSGGSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYTF 92
Cdd:PRK11706    2 IPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  93 CATATAFARKGARIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAKQ 172
Cdd:PRK11706   82 VSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 173 DGRAVGTCGLFAAYSFHETKIISAGHGGALVLNSDNshLRERVEELLARGTNFPAFARGEVNHYEWTSVSSSFEMPDLNA 252
Cdd:PRK11706  162 KGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPA--LIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 253 ALLYSQLVHSREILLKSRAIWAYYEKSLRDLP----IEILRPGKGTKANGYSFAFLAKDRETTYRILQGAARMGLGLQSH 328
Cdd:PRK11706  240 AYLWAQLEAADRINQRRLALWQRYYDALAPLAeagrIELPSIPDDCKHNAHMFYIKLRDLEDRSALINFLKEAGIMAVFH 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1148544270 329 YKPLHlSSFAGRIL---AGSCVGAENTWGRLVRLPVHMDLSTGDAARICEFLKA 379
Cdd:PRK11706  320 YIPLH-SSPAGERFgrfHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILE 372
 
Name Accession Description Interval E-value
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 13-379 1.88e-118

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 348.36  E-value: 1.88e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  13 IRFHAPHIPPATYDAVASALSSKHLRSGGSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYTF 92
Cdd:PRK11706    2 IPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  93 CATATAFARKGARIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAKQ 172
Cdd:PRK11706   82 VSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 173 DGRAVGTCGLFAAYSFHETKIISAGHGGALVLNSDNshLRERVEELLARGTNFPAFARGEVNHYEWTSVSSSFEMPDLNA 252
Cdd:PRK11706  162 KGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPA--LIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 253 ALLYSQLVHSREILLKSRAIWAYYEKSLRDLP----IEILRPGKGTKANGYSFAFLAKDRETTYRILQGAARMGLGLQSH 328
Cdd:PRK11706  240 AYLWAQLEAADRINQRRLALWQRYYDALAPLAeagrIELPSIPDDCKHNAHMFYIKLRDLEDRSALINFLKEAGIMAVFH 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1148544270 329 YKPLHlSSFAGRIL---AGSCVGAENTWGRLVRLPVHMDLSTGDAARICEFLKA 379
Cdd:PRK11706  320 YIPLH-SSPAGERFgrfHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILE 372
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
12-381 8.18e-107

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 318.17  E-value: 8.18e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  12 PIRFHAPHIPPATYDAVASALSSKHLrSGGSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYT 91
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWL-TLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  92 FCATATAFARKGARIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAK 171
Cdd:COG0399    80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 172 QDGRAVGTCGLFAAYSFHETKIISAGHGGALVLNSDNshLRERVEELLARGtnfpafaRGEVNHYEWTSVSSSFEMPDLN 251
Cdd:COG0399   160 YKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEE--LAERARSLRNHG-------RDRDAKYEHVELGYNYRMDELQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 252 AALLYSQLVHSREILLKSRAIWAYYEKSLRDLP-IEILRPGKGTKANGYSFAFLAKDRETTYRILQGAARMGLGLQSHY- 329
Cdd:COG0399   231 AAIGLAQLKRLDEFIARRRAIAARYREALADLPgLTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKARGIGTRVHYp 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1148544270 330 KPLHLSS-FAGRIL-AGSCVGAENTWGRLVRLPVHMDLSTGDAARICEFLKAEL 381
Cdd:COG0399   311 IPLHLQPaYRDLGYrPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 25-378 1.95e-94

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 286.36  E-value: 1.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  25 YDAVASALSSKHLrSGGSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYTFCATATAFARKGA 104
Cdd:cd00616     2 LEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 105 RIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAKQDGRAVGTCGLFA 184
Cdd:cd00616    81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 185 AYSFHETKIISAGHGGALVLNsdNSHLRERVEELLARGTnfpafaRGEVNHYEWTSVSSSFEMPDLNAALLYSQLVHSRE 264
Cdd:cd00616   161 AFSFHPTKNLTTGEGGAVVTN--DEELAERARLLRNHGR------DRDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 265 ILLKSRAIWAYYEKSLRDLP-IEILRPGKGTKANGYSFAFL-----AKDRETTYRILQGAarmGLGLQSHYKPLHLSSFA 338
Cdd:cd00616   233 IIARRREIAERYKELLADLPgIRLPDVPPGVKHSYHLYVIRldpeaGESRDELIEALKEA---GIETRVHYPPLHHQPPY 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1148544270 339 GRILA---GSCVGAENTWGRLVRLPVHMDLSTGDAARICEFLK 378
Cdd:cd00616   310 KKLLGyppGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
ECA_wecE TIGR02379
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ...
 13-377 1.56e-91

TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of TDP-4-keto-6-deoxy-D-glucose transaminases, the WecE (formerly RffA) protein of enterobacterial common antigen (ECA) biosynthesis, from enterobacteria. It also includes closely matching sequence from species not expected to make ECA, but which contain other genes for the biosynthesis of TDP-4-keto-6-deoxy-D-Glc, an intermediate in the biosynthesis of other compounds as well and the substrate of WecA. This family belongs to the DegT/DnrJ/EryC1/StrS aminotransferase family (pfam01041). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131432  Cd Length: 376  Bit Score: 279.78  E-value: 1.56e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  13 IRFHAPHIPPATYDAVASALSSKHLRSGGSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYTF 92
Cdd:TIGR02379   2 IPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYTF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  93 CATATAFARKGARIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAKQ 172
Cdd:TIGR02379  82 VSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMSTY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 173 DGRAVGTCGLFAAYSFHETK-IISAGHGGALVLNSDNshLRERVEELLARGTNFPAFARGEVNHYEWTSVSSSFEMPDLN 251
Cdd:TIGR02379 162 KGRALGSIGHIGTFSFHETKnYTSGGEGGALLINDQA--FIERAEIIREKGTNRSQFFRGEVDKYTWRDIGSSYLPSELQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 252 AALLYSQLVHSREILLKSRAIWAYYEKSLrdLPIE----ILRPG--KGTKANGYSFAFLAKDRETTYRILQGAARMGLGL 325
Cdd:TIGR02379 240 AAYLWAQLEQADRINQQRLALWQNYYDAL--APLEekgiIELPSipDGCQHNAHMFYIKLRDIDDRSELINFLKEQEIMA 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1148544270 326 QSHYKPLHlSSFAGRILA---GSCVGAENTWGRLVRLPVHMDLSTGDAARICEFL 377
Cdd:TIGR02379 318 VFHYIPLH-SSPAGRHFGrfhGEDIYTTKESERLVRLPLFYGLSPEDQRRVIATL 371
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 26-378 7.25e-81

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 251.82  E-value: 7.25e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  26 DAVASALSSKHLRSGgSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYTFCATATAFARKGAR 105
Cdd:pfam01041   9 AAVREVLKSGWLTTG-PYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAALRLGAK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 106 IVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAKQDGRAVGTCGLFAA 185
Cdd:pfam01041  88 PVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLGDAAT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 186 YSFHETKIISAGHGGALVLNSDNshLRERVEELLARGtnfpaFARGEVNHYEWTSVSSSFEMPDLNAALLYSQLVHSREI 265
Cdd:pfam01041 168 FSFHPTKNLTTGEGGAVVTNDPE--LAEKARVLRNHG-----MVRKADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDEF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 266 LLKSRAIWAYYEKSLRDLPiEILRPGKGTKANGYS---FAFLAKDRETTYRILQGA-ARMGLGLQSHY-KPLHLSSF--- 337
Cdd:pfam01041 241 IARRREIAALYQTLLADLP-GFTPLTTPPEADVHAwhlFPILVPEEAINRDELVEAlKEAGIGTRVHYpIPLHLQPYyrd 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1148544270 338 AGRILAGSCVGAENTWGRLVRLPVHMDLSTGDAARICEFLK 378
Cdd:pfam01041 320 LFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
 
Name Accession Description Interval E-value
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 13-379 1.88e-118

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 348.36  E-value: 1.88e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  13 IRFHAPHIPPATYDAVASALSSKHLRSGGSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYTF 92
Cdd:PRK11706    2 IPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  93 CATATAFARKGARIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAKQ 172
Cdd:PRK11706   82 VSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 173 DGRAVGTCGLFAAYSFHETKIISAGHGGALVLNSDNshLRERVEELLARGTNFPAFARGEVNHYEWTSVSSSFEMPDLNA 252
Cdd:PRK11706  162 KGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPA--LIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 253 ALLYSQLVHSREILLKSRAIWAYYEKSLRDLP----IEILRPGKGTKANGYSFAFLAKDRETTYRILQGAARMGLGLQSH 328
Cdd:PRK11706  240 AYLWAQLEAADRINQRRLALWQRYYDALAPLAeagrIELPSIPDDCKHNAHMFYIKLRDLEDRSALINFLKEAGIMAVFH 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1148544270 329 YKPLHlSSFAGRIL---AGSCVGAENTWGRLVRLPVHMDLSTGDAARICEFLKA 379
Cdd:PRK11706  320 YIPLH-SSPAGERFgrfHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILE 372
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
12-381 8.18e-107

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 318.17  E-value: 8.18e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  12 PIRFHAPHIPPATYDAVASALSSKHLrSGGSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYT 91
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWL-TLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  92 FCATATAFARKGARIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAK 171
Cdd:COG0399    80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 172 QDGRAVGTCGLFAAYSFHETKIISAGHGGALVLNSDNshLRERVEELLARGtnfpafaRGEVNHYEWTSVSSSFEMPDLN 251
Cdd:COG0399   160 YKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEE--LAERARSLRNHG-------RDRDAKYEHVELGYNYRMDELQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 252 AALLYSQLVHSREILLKSRAIWAYYEKSLRDLP-IEILRPGKGTKANGYSFAFLAKDRETTYRILQGAARMGLGLQSHY- 329
Cdd:COG0399   231 AAIGLAQLKRLDEFIARRRAIAARYREALADLPgLTLPKVPPGAEHVYHLYVIRLDEGEDRDELIAALKARGIGTRVHYp 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1148544270 330 KPLHLSS-FAGRIL-AGSCVGAENTWGRLVRLPVHMDLSTGDAARICEFLKAEL 381
Cdd:COG0399   311 IPLHLQPaYRDLGYrPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 25-378 1.95e-94

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 286.36  E-value: 1.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  25 YDAVASALSSKHLrSGGSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYTFCATATAFARKGA 104
Cdd:cd00616     2 LEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 105 RIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAKQDGRAVGTCGLFA 184
Cdd:cd00616    81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 185 AYSFHETKIISAGHGGALVLNsdNSHLRERVEELLARGTnfpafaRGEVNHYEWTSVSSSFEMPDLNAALLYSQLVHSRE 264
Cdd:cd00616   161 AFSFHPTKNLTTGEGGAVVTN--DEELAERARLLRNHGR------DRDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 265 ILLKSRAIWAYYEKSLRDLP-IEILRPGKGTKANGYSFAFL-----AKDRETTYRILQGAarmGLGLQSHYKPLHLSSFA 338
Cdd:cd00616   233 IIARRREIAERYKELLADLPgIRLPDVPPGVKHSYHLYVIRldpeaGESRDELIEALKEA---GIETRVHYPPLHHQPPY 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1148544270 339 GRILA---GSCVGAENTWGRLVRLPVHMDLSTGDAARICEFLK 378
Cdd:cd00616   310 KKLLGyppGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
ECA_wecE TIGR02379
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ...
 13-377 1.56e-91

TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of TDP-4-keto-6-deoxy-D-glucose transaminases, the WecE (formerly RffA) protein of enterobacterial common antigen (ECA) biosynthesis, from enterobacteria. It also includes closely matching sequence from species not expected to make ECA, but which contain other genes for the biosynthesis of TDP-4-keto-6-deoxy-D-Glc, an intermediate in the biosynthesis of other compounds as well and the substrate of WecA. This family belongs to the DegT/DnrJ/EryC1/StrS aminotransferase family (pfam01041). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131432  Cd Length: 376  Bit Score: 279.78  E-value: 1.56e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  13 IRFHAPHIPPATYDAVASALSSKHLRSGGSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYTF 92
Cdd:TIGR02379   2 IPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYTF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  93 CATATAFARKGARIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAKQ 172
Cdd:TIGR02379  82 VSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMSTY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 173 DGRAVGTCGLFAAYSFHETK-IISAGHGGALVLNSDNshLRERVEELLARGTNFPAFARGEVNHYEWTSVSSSFEMPDLN 251
Cdd:TIGR02379 162 KGRALGSIGHIGTFSFHETKnYTSGGEGGALLINDQA--FIERAEIIREKGTNRSQFFRGEVDKYTWRDIGSSYLPSELQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 252 AALLYSQLVHSREILLKSRAIWAYYEKSLrdLPIE----ILRPG--KGTKANGYSFAFLAKDRETTYRILQGAARMGLGL 325
Cdd:TIGR02379 240 AAYLWAQLEQADRINQQRLALWQNYYDAL--APLEekgiIELPSipDGCQHNAHMFYIKLRDIDDRSELINFLKEQEIMA 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1148544270 326 QSHYKPLHlSSFAGRILA---GSCVGAENTWGRLVRLPVHMDLSTGDAARICEFL 377
Cdd:TIGR02379 318 VFHYIPLH-SSPAGRHFGrfhGEDIYTTKESERLVRLPLFYGLSPEDQRRVIATL 371
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 26-378 7.25e-81

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 251.82  E-value: 7.25e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  26 DAVASALSSKHLRSGgSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYTFCATATAFARKGAR 105
Cdd:pfam01041   9 AAVREVLKSGWLTTG-PYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANAALRLGAK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 106 IVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAKQDGRAVGTCGLFAA 185
Cdd:pfam01041  88 PVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLGDAAT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 186 YSFHETKIISAGHGGALVLNSDNshLRERVEELLARGtnfpaFARGEVNHYEWTSVSSSFEMPDLNAALLYSQLVHSREI 265
Cdd:pfam01041 168 FSFHPTKNLTTGEGGAVVTNDPE--LAEKARVLRNHG-----MVRKADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDEF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 266 LLKSRAIWAYYEKSLRDLPiEILRPGKGTKANGYS---FAFLAKDRETTYRILQGA-ARMGLGLQSHY-KPLHLSSF--- 337
Cdd:pfam01041 241 IARRREIAALYQTLLADLP-GFTPLTTPPEADVHAwhlFPILVPEEAINRDELVEAlKEAGIGTRVHYpIPLHLQPYyrd 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1148544270 338 AGRILAGSCVGAENTWGRLVRLPVHMDLSTGDAARICEFLK 378
Cdd:pfam01041 320 LFGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
22-288 1.37e-46

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 163.27  E-value: 1.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  22 PATYDAVASALSsKHLRSG----GSYSRKAKALVSQHVGHDRVFLTNSCTSALEISALALDLGPEDEVIVPSYTFCATAT 97
Cdd:PRK11658   10 PAMGDEELAAVK-EVLRSGwittGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTLN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  98 AFARKGARIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVVILEDAAQAFGAKQDGRAV 177
Cdd:PRK11658   89 MIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGRHI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 178 GTCGLfAAYSFHETKIISAGHGGALVlnSDNSHLRERVEELLARGTNFPAFAR---GEVNHYEWTSVSSSFEMPDLNAAL 254
Cdd:PRK11658  169 GARGT-AIFSFHAIKNITCAEGGLVV--TDDDELADRLRSLKFHGLGVDAFDRqtqGRAPQAEVLTPGYKYNLADINAAI 245

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1148544270 255 LYSQLVHSREILLKSRAIWAYYEKSLRDLPIEIL 288
Cdd:PRK11658  246 ALVQLAKLEALNARRREIAARYLQALADLPFQPL 279
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 7-216 1.97e-24

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 103.81  E-value: 1.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270   7 EAALPPIRFHAP--HIPPA--TYDA------VASALSSkHLRSGGsYSRKAKALVSQHVGHDRVFLTNSCTSA--LEISA 74
Cdd:PRK15407   20 ELAHAPKPFVPGksPIPPSgkVIDAkelqnlVDASLDF-WLTTGR-FNDAFEKKLAEFLGVRYALLVNSGSSAnlLAFSA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  75 L-ALDLG-----PEDEVIVPSYTFCATATAFARKGARIVLADIDPGTMMVTPETLEARLTSRTRAVVVVHYGGAAAPMAA 148
Cdd:PRK15407   98 LtSPKLGdralkPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAA 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148544270 149 IKDLCDRHGVVILEDAAQAFGAKQDGRAVGTCGLFAAYSFHETKIISAGHGGALVLNsdNSHLRERVE 216
Cdd:PRK15407  178 VKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTN--DPLLKKIIE 243
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 56-170 4.30e-14

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 69.72  E-value: 4.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  56 GHDRVFLTNSCTSALEISALALdLGPEDEVIVPSYTFCATATAFA-RKGARIVLADIDPGTMMV-TPETLEARLTSRTRA 133
Cdd:cd01494    16 GNDKAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRYWVAAeLAGAKPVPVPVDDAGYGGlDVAILEELKAKPNVA 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1148544270 134 VVVVHY----GGAAAPMAAIKDLCDRHGVVILEDAAQAFGA 170
Cdd:cd01494    95 LIVITPnttsGGVLVPLKEIRKIAKEYGILLLVDAASAGGA 135
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 21-165 8.82e-14

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 71.60  E-value: 8.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  21 PPATYDAVASALSSKHLRSGGsysrkakalvsQHVGHDRVFLTNSCTSALEISALALdLGPEDEVIVPSYTFCATATAFA 100
Cdd:cd00609    34 PDPGLPELREAIAEWLGRRGG-----------VDVPPEEIVVTNGAQEALSLLLRAL-LNPGDEVLVPDPTYPGYEAAAR 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148544270 101 RKGARIVLADIDP-GTMMVTPETLEARLTSRTRAVVVVHYG---GAAAP---MAAIKDLCDRHGVVILEDAA 165
Cdd:cd00609   102 LAGAEVVPVPLDEeGGFLLDLELLEAAKTPKTKLLYLNNPNnptGAVLSeeeLEELAELAKKHGILIISDEA 173
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 21-163 3.19e-13

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 70.16  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  21 PPATYDAVASALSSKHLR---SGGSYS-RKAkalVSQH--------VGHDRVFLTNSCTSALEISALALdLGPEDEVIVP 88
Cdd:COG0436    45 PDHIREAAIEALDDGVTGytpSAGIPElREA---IAAYykrrygvdLDPDEILVTNGAKEALALALLAL-LNPGDEVLVP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  89 -----SYTFCATATafarkGARIVLADIDPGT-MMVTPETLEARLTSRTRAVVVVHYG---GAAAP---MAAIKDLCDRH 156
Cdd:COG0436   121 dpgypSYRAAVRLA-----GGKPVPVPLDEENgFLPDPEALEAAITPRTKAIVLNSPNnptGAVYSreeLEALAELAREH 195


                  ....*..
gi 1148544270 157 GVVILED 163
Cdd:COG0436   196 DLLVISD 202
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
46-169 3.35e-11

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 64.00  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  46 KAKALVSQHVG---HDRVFLTNSCTSALEISALALD-LGPEDEVIVPSYTFCATATAF----ARKGARIVLADIDP-GTm 116
Cdd:COG0520    63 AAREKVARFIGaasPDEIIFTRGTTEAINLVAYGLGrLKPGDEILITEMEHHSNIVPWqelaERTGAEVRVIPLDEdGE- 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1148544270 117 mVTPETLEARLTSRTRAVVVVH---YGGAAAPMAAIKDLCDRHGVVILEDAAQAFG 169
Cdd:COG0520   142 -LDLEALEALLTPRTKLVAVTHvsnVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 58-167 1.73e-09

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 58.63  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  58 DRVFLTNSCTSALEI--SALALDLGPEDEV----------IVPSYTFCAtatafaRKGARIVLADIDP-GTmmVTPETLE 124
Cdd:cd06453    62 DEIIFTRNTTEAINLvaYGLGRANKPGDEIvtsvmehhsnIVPWQQLAE------RTGAKLKVVPVDDdGQ--LDLEALE 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1148544270 125 ARLTSRTRAVVVVH---YGGAAAPMAAIKDLCDRHGVVILEDAAQA 167
Cdd:cd06453   134 KLLTERTKLVAVTHvsnVLGTINPVKEIGEIAHEAGVPVLVDGAQS 179
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 19-290 6.37e-08

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 53.79  E-value: 6.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  19 HIPPATYDAV--------ASALSSKHLRSGGSYS--RKAKALVSQHVG---HDRVFLTNSCTSALEISALAL--DLGPED 83
Cdd:pfam00266  10 QKPQEVLDAIqeyytdynGNVHRGVHTLGKEATQayEEAREKVAEFINapsNDEIIFTSGTTEAINLVALSLgrSLKPGD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  84 EVIV-----PSYTFCATATAfARKGARIVLADIDPGTMmVTPETLEARLTSRTRAVVVVHYG---GAAAPMAAIKDLCDR 155
Cdd:pfam00266  90 EIVItemehHANLVPWQELA-KRTGARVRVLPLDEDGL-LDLDELEKLITPKTKLVAITHVSnvtGTIQPVPEIGKLAHQ 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 156 HGVVILEDAAQAFG-AKQDGRAVGtCGlFAAYSFHetKIISAGHGGALVLNSDnshLRERVEELLARGTNfpaFARGEVN 234
Cdd:pfam00266 168 YGALVLVDAAQAIGhRPIDVQKLG-VD-FLAFSGH--KLYGPTGIGVLYGRRD---LLEKMPPLLGGGGM---IETVSLQ 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1148544270 235 HYEWTSVSSSFEM--PD------LNAALLYSQLVHSREILLKSRAIWAYYEKSLRDLP-IEILRP 290
Cdd:pfam00266 238 ESTFADAPWKFEAgtPNiagiigLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPgIRLYGP 302
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 54-163 1.60e-07

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440781 [Multi-domain]  Cd Length: 471  Bit Score: 52.91  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  54 HVGHDRVFLTNSCTSALEISALALdLGPEDEVIVPSYTFCATATAFARKGARIVLADIDPGTMmvTPETLEARL-TSRTR 132
Cdd:COG1167   167 PASPDQILITSGAQQALDLALRAL-LRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGL--DLDALEAALrRHRPR 243

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1148544270 133 AVVVV---HY-GGAAAPMA---AIKDLCDRHGVVILED 163
Cdd:COG1167   244 AVYVTpshQNpTGATMSLErrrALLELARRHGVPIIED 281
PRK07550 PRK07550
aminotransferase;
21-203 4.00e-07

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 51.50  E-value: 4.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  21 PPATYDAVASALSS------------KHLRsgGSYSRKAKALVSQHVGHDRVFLTNSCTSA--LEISALAldlGPEDEVI 86
Cdd:PRK07550   44 PPELLRALAEAAADpaahlygpveglPELR--EAYAAHYSRLYGAAISPEQVHITSGCNQAfwAAMVTLA---GAGDEVI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  87 VPSYTFCATATAFARKGARIVLADIDPG-TMMVTPETLEARLTSRTRAVVVV---HYGGAAAP---MAAIKDLCDRHGV- 158
Cdd:PRK07550  119 LPLPWYFNHKMWLDMLGIRPVYLPCDEGpGLLPDPAAAEALITPRTRAIALVtpnNPTGVVYPpelLHELYDLARRHGIa 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1148544270 159 VILEDAAQAFgakqDGRAVGTCGLFAA----------YSFHETKIISAGHGGALV 203
Cdd:PRK07550  199 LILDETYRDF----DSGGGAPHDLFADpdwddtlvhlYSFSKSYALTGHRVGAVV 249
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 74-163 1.81e-06

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 49.35  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  74 ALALDLGPEDEVIVP-----SYtfcATATAFArkGARIVLADIDPGT-MMVTPETLEARLTSRTRAVVVVH----YGGAA 143
Cdd:PRK05764  107 AFMALLDPGDEVIIPapywvSY---PEMVKLA--GGVPVFVPTGEENgFKLTVEQLEAAITPKTKALILNSpsnpTGAVY 181

                          90       100
                  ....*....|....*....|..
gi 1148544270 144 AP--MAAIKDLCDRHGVVILED 163
Cdd:PRK05764  182 SPeeLEAIADVAVEHDIWVLSD 203
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
58-163 4.11e-06

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 48.40  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  58 DRVFLTNSCTSALEISALALdLGPEDEVIVPSYTFCATATAFARKGARIVLADIDP--GTMMVTPETLEARLTSRTRAVV 135
Cdd:PRK06108   85 ERIAVTSSGVQALMLAAQAL-VGPGDEVVAVTPLWPNLVAAPKILGARVVCVPLDFggGGWTLDLDRLLAAITPRTRALF 163

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1148544270 136 V------VHYGGAAAPMAAIKDLCDRHGVVILED 163
Cdd:PRK06108  164 InspnnpTGWTASRDDLRAILAHCRRHGLWIVAD 197
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 94-169 1.97e-05

Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];


Pssm-ID: 440721 [Multi-domain]  Cd Length: 381  Bit Score: 46.19  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  94 ATATAFARKGARIVLADIDP-GtmMVTPETLEARLTSRTrAVVVVHYG----GAAAPMAAIKDLCDRHGVVILEDAAQAF 168
Cdd:COG1104   105 ETARFLEKEGFEVTYLPVDEdG--RVDLEALEAALRPDT-ALVSVMHAnnetGTIQPIAEIAEIAKEHGVLFHTDAVQAV 181


                  .
gi 1148544270 169 G 169
Cdd:COG1104   182 G 182
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
54-163 2.20e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 46.00  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  54 HVGHDRVFLTNSCTSALEISALALdLGPEDEVIVPSyTFCATATAFARK-GARI--VLADIDPGTMMVTPETLEARLTSR 130
Cdd:PRK07568   85 DVEPDEILITNGGSEAILFAMMAI-CDPGDEILVPE-PFYANYNGFATSaGVKIvpVTTKIEEGFHLPSKEEIEKLITPK 162

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1148544270 131 TRAVVVVHYG---GA---AAPMAAIKDLCDRHGVVILED 163
Cdd:PRK07568  163 TKAILISNPGnptGVvytKEELEMLAEIAKKHDLFLISD 201
PRK05855 PRK05855
SDR family oxidoreductase;
94-159 5.22e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 45.36  E-value: 5.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148544270  94 ATATAFARKGARIVLADIDPGTMMVTPEtlEARLTSRTRAVVVVHYGGAAAPMAAIKDLCDRHGVV 159
Cdd:PRK05855  330 ETALAFAREGAEVVASDIDEAAAERTAE--LIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVP 393
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
21-186 6.97e-05

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 44.60  E-value: 6.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  21 PPATYDAVASALSSKHLRSGGSYSRKAKALVsqhvghdrvflTNSCTSALEISALALDLGPEDEVIVPSYTFCATATAF- 99
Cdd:pfam00155  37 PTDGHPELREALAKFLGRSPVLKLDREAAVV-----------FGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIAr 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 100 ARKGARIVLADIDPGTMMVTPETLEARLTSRTraVVVVHYG-----GAAAPMAAIKDL---CDRHGVVILEDAAQAFGAK 171
Cdd:pfam00155 106 LAGGEVVRYPLYDSNDFHLDFDALEAALKEKP--KVVLHTSphnptGTVATLEELEKLldlAKEHNILLLVDEAYAGFVF 183

                         170
                  ....*....|....*
gi 1148544270 172 QDGRAVGTCGLFAAY 186
Cdd:pfam00155 184 GSPDAVATRALLAEG 198
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
22-136 2.03e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 42.87  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  22 PATYDAVASALSSKHlrsggsysrkakalvSQHVGHDRVFLTNSCTSALEISALALdLGPEDEVIVPS-----YTFCATA 96
Cdd:PRK06836   76 PEVREAIAESLNRRF---------------GTPLTADHIVMTCGAAGALNVALKAI-LNPGDEVIVFApyfveYRFYVDN 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1148544270  97 TafarkGARIVLADIDPGTMMVTPETLEARLTSRTRAVVV 136
Cdd:PRK06836  140 H-----GGKLVVVPTDTDTFQPDLDALEAAITPKTKAVII 174
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 62-170 3.90e-04

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 42.28  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  62 LTNSCTSALEiSALALDLGPEDEVIVpsytfcATATAFA--------RKGARIVLADIDPGTMmVTPETLEARLTSRT-R 132
Cdd:cd06451    55 LSGSGTGAME-AALSNLLEPGDKVLV------GVNGVFGdrwadmaeRYGADVDVVEKPWGEA-VSPEEIAEALEQHDiK 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1148544270 133 AVVVVH---YGGAAAPMAAIKDLCDRHGVVILEDAAQAFGA 170
Cdd:cd06451   127 AVTLTHnetSTGVLNPLEGIGALAKKHDALLIVDAVSSLGG 167
PLN00175 PLN00175
aminotransferase family protein; Provisional
 60-163 4.02e-04

aminotransferase family protein; Provisional


Pssm-ID: 215089 [Multi-domain]  Cd Length: 413  Bit Score: 42.16  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  60 VFLTNSCTSALEISALALdLGPEDEVIV--PSYTFCATATAFArkGARIVLADIDPGTMMVTPETLEARLTSRTRAVVVV 137
Cdd:PLN00175  118 VTVTSGCTEAIAATILGL-INPGDEVILfaPFYDSYEATLSMA--GAKIKTVTLRPPDFAVPEDELKAAFTSKTRAILIN 194

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1148544270 138 HYGGAAAPM------AAIKDLCDRHGVVILED 163
Cdd:PLN00175  195 TPHNPTGKMftreelELIASLCKENDVLAFTD 226
PRK06139 PRK06139
SDR family oxidoreductase;
94-193 7.66e-04

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 41.24  E-value: 7.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  94 ATATAFARKGARIVLADIDPGTMMVTPETLEARltsrtravvvvhygGAAApMAAIKDLCDRHGVVILEDAAQAFGAKQD 173
Cdd:PRK06139   22 ATAEAFARRGARLVLAARDEEALQAVAEECRAL--------------GAEV-LVVPTDVTDADQVKALATQAASFGGRID 86

                          90       100
                  ....*....|....*....|
gi 1148544270 174 gRAVGTCGLFAAYSFHETKI 193
Cdd:PRK06139   87 -VWVNNVGVGAVGRFEETPI 105
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
56-165 1.16e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 40.83  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  56 GHDRVFLTNSCTSALEISALALdLGPEDEVIVPSYTFCATATAFARKGARIVLADIDPGtMMVTPETLEARLTSRTRAVV 135
Cdd:PRK05957   88 NEQAIVVTAGSNMAFMNAILAI-TDPGDEIILNTPYYFNHEMAITMAGCQPILVPTDDN-YQLQPEAIEQAITPKTRAIV 165

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1148544270 136 VV---HYGGAAAP---MAAIKDLCDRHGVVILEDAA 165
Cdd:PRK05957  166 TIspnNPTGVVYPealLRAVNQICAEHGIYHISDEA 201
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 43-222 1.16e-03

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 40.39  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  43 YSRKAKALVSQHVGHDRVFLTNSCTSALEISALALdLGPEDEVIVPS----YTFCATATAFArKGARIVLADIDPGTMmv 118
Cdd:cd06502    33 TTAKLEARAAELFGKEAALFVPSGTAANQLALAAH-TQPGGSVICHEtahiYTDEAGAPEFL-SGVKLLPVPGENGKL-- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 119 TPETLEARLT-------SRTRAVVV--VHYGGAAAP---MAAIKDLCDRHGVVILEDAAQAFGA-KQDGRAVGT-CGLFA 184
Cdd:cd06502   109 TPEDLEAAIRprddihfPPPSLVSLenTTEGGTVYPldeLKAISALAKENGLPLHLDGARLANAaAALGVALKTyKSGVD 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1148544270 185 AYSFHETKIISAGHGGALVLN----SDNSHLRERVEELLARG 222
Cdd:cd06502   189 SVSFCLSKGGGAPVGAVVVGNrdfiARARRRRKQAGGGMRQS 230
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 45-219 1.72e-03

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 39.92  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  45 RKAKALVSQHVGHDRVF-LTNSCTSALEISALALdLGPEDEVIVPSYTFCATATAFARKGAR--IVLADIDPGTMM---V 118
Cdd:cd00615    62 KEAQELAARAFGAKHTFfLVNGTSSSNKAVILAV-CGPGDKILIDRNCHKSVINGLVLSGAVpvYLKPERNPYYGIaggI 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270 119 TPETLEARLTSRTRAVVVV----HYGGAAAPMAAIKDLCDRHGVVILEDAAQ----AFGAKQDGRAVGTCGLFAAYSFHe 190
Cdd:cd00615   141 PPETFKKALIEHPDAKAAVitnpTYYGICYNLRKIVEEAHHRGLPVLVDEAHgahfRFHPILPSSAAMAGADIVVQSTH- 219

                         170       180
                  ....*....|....*....|....*....
gi 1148544270 191 tKIISAGHGGALVLNSDNSHLRERVEELL 219
Cdd:cd00615   220 -KTLPALTQGSMIHVKGDLVNPDRVNEAL 247
PLN02651 PLN02651
cysteine desulfurase
 117-169 2.00e-03

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 40.02  E-value: 2.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1148544270 117 MVTPETLEARLTSRTRAVVVVHYG---GAAAPMAAIKDLCDRHGVVILEDAAQAFG 169
Cdd:PLN02651  125 LVDLDELAAAIRPDTALVSVMAVNneiGVIQPVEEIGELCREKKVLFHTDAAQAVG 180
PRK09295 PRK09295
cysteine desulfurase SufS;
86-167 2.17e-03

cysteine desulfurase SufS;


Pssm-ID: 181766 [Multi-domain]  Cd Length: 406  Bit Score: 39.73  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  86 IVPSYTFCAtatafaRKGARIVLADIDP-GTMMVtpETLEARLTSRTRAVVVVHYG---GAAAPMAAIKDLCDRHGVVIL 161
Cdd:PRK09295  127 IVPWQMLCA------RVGAELRVIPLNPdGTLQL--ETLPALFDERTRLLAITHVSnvlGTENPLAEMIALAHQHGAKVL 198


                  ....*.
gi 1148544270 162 EDAAQA 167
Cdd:PRK09295  199 VDGAQA 204
PRK09265 PRK09265
aminotransferase AlaT; Validated
 39-163 7.39e-03

aminotransferase AlaT; Validated


Pssm-ID: 181738  Cd Length: 404  Bit Score: 38.25  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148544270  39 SGGSYS-RKAkalVSQH--------VGHDRVFLTNSCTSALEISALALdLGPEDEVIVPS--YTFCATATAFArkGARIV 107
Cdd:PRK09265   71 SKGLFSaRKA---IMQYyqqkgipdVDVDDIYIGNGVSELIVMAMQAL-LNNGDEVLVPApdYPLWTAAVSLS--GGKPV 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148544270 108 --LADIDPGtMMVTPETLEARLTSRTRAVVVVHYG---GAAAPMA---AIKDLCDRHGVVILED 163
Cdd:PRK09265  145 hyLCDEEAG-WFPDLDDIRSKITPRTKAIVIINPNnptGAVYSKElleEIVEIARQHNLIIFAD 207
 
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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