|
Name |
Accession |
Description |
Interval |
E-value |
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
28-408 |
0e+00 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 513.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 28 PKLTDEEKQLVLDVLDSGRLvsSIGKYVKLFEEEFARYLGVRHAVATINGTASLHTAVASLNIGPGDEVITTPFSFIATA 107
Cdd:COG0399 7 PSIGEEEIAAVVEVLRSGWL--TLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 108 TSILHNNAVPVFADIEKDSLNLDPATIEEKITPRTKAILVVHLAGYPAEMDEILKIAREHNLYVIEDCAQAIGSEYRGRK 187
Cdd:COG0399 85 NAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 188 VGTFGDINAFSFYQTKNMTTGEGGMVTTDKEELYRYAKMFVDQGQE--SKYYHTILGWNYRMTELQAALGLGQLRRIGEL 265
Cdd:COG0399 165 VGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDrdAKYEHVELGYNYRMDELQAAIGLAQLKRLDEF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 266 NAAREKIAQIYMDELSSLNGdlLKLPVLKPYVKHTWHIFQVLLnldKLRVNRDRIIEALKAENVLVQVVYPRVIYENPLF 345
Cdd:COG0399 245 IARRRAIAARYREALADLPG--LTLPKVPPGAEHVYHLYVIRL---DEGEDRDELIAALKARGIGTRVHYPIPLHLQPAY 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203628960 346 QRLtgygkgcpwlcpfygkqiTYKKGSSPIAEQVARSVITLPTLPGMTEEDAIDTANAIKKVL 408
Cdd:COG0399 320 RDL------------------GYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
34-405 |
5.55e-169 |
|
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: 477.03 E-value: 5.55e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 34 EKQLVLDVLDSGRLvsSIGKYVKLFEEEFARYLGVRHAVATINGTASLHTAVASLNIGPGDEVITTPFSFIATATSILHN 113
Cdd:cd00616 1 ELEAVEEVLDSGWL--TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 114 NAVPVFADIEKDSLNLDPATIEEKITPRTKAILVVHLAGYPAEMDEILKIAREHNLYVIEDCAQAIGSEYRGRKVGTFGD 193
Cdd:cd00616 79 GATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 194 INAFSFYQTKNMTTGEGGMVTTDKEELYRYAKMFVDQGQES---KYYHTILGWNYRMTELQAALGLGQLRRIGELNAARE 270
Cdd:cd00616 159 AGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRdrfKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 271 KIAQIYMDELSSLNGdlLKLPVLKPYVKHTWHIFQVLLNlDKLRVNRDRIIEALKAENVLVQVVYPrviyenPLFQRltg 350
Cdd:cd00616 239 EIAERYKELLADLPG--IRLPDVPPGVKHSYHLYVIRLD-PEAGESRDELIEALKEAGIETRVHYP------PLHHQ--- 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2203628960 351 ygkgcpwlcPFYGKQITYKKGSSPIAEQVARSVITLPTLPGMTEEDAIDTANAIK 405
Cdd:cd00616 307 ---------PPYKKLLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
28-405 |
1.39e-153 |
|
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: 438.26 E-value: 1.39e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 28 PKLTDEEKQLVLDVLDSGRLVSsiGKYVKLFEEEFARYLGVRHAVATINGTASLHTAVASLNIGPGDEVITTPFSFIATA 107
Cdd:pfam01041 1 PDIDEEELAAVREVLKSGWLTT--GPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 108 TSILHNNAVPVFADIEKDSLNLDPATIEEKITPRTKAILVVHLAGYPAEMDEILKIAREHNLYVIEDCAQAIGSEYRGRK 187
Cdd:pfam01041 79 NAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 188 VGTFGDINAFSFYQTKNMTTGEGGMVTTDKEELYRYAKMFVDQG----QESKYYHTILGWNYRMTELQAALGLGQLRRIG 263
Cdd:pfam01041 159 VGTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGmvrkADKRYWHEVLGYNYRMTEIQAAIGLAQLERLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 264 ELNAAREKIAQIYMDELSSLNGDLLkLPVLKPYVKHTWHIFQVLlnLDKLRVNRDRIIEALKAENVLVQVVYPRVIYENP 343
Cdd:pfam01041 239 EFIARRREIAALYQTLLADLPGFTP-LTTPPEADVHAWHLFPIL--VPEEAINRDELVEALKEAGIGTRVHYPIPLHLQP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203628960 344 LFQRLTGygkgcpwlcpfygkqitYKKGSSPIAEQVARSVITLPTLPGMTEEDAIDTANAIK 405
Cdd:pfam01041 316 YYRDLFG-----------------YAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
|
|
| NHT_00031 |
TIGR04181 |
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the ... |
28-387 |
1.69e-112 |
|
aminotransferase, LLPSF_NHT_00031 family; This clade of aminotransferases is a member of the pfam01041 (DegT/DnrJ/EryC1/StrS) superfamily. The family is named after the instance in Leptospira interrogans serovar Lai, str. 56601, where it is the 31st gene in the 91-gene lipopolysaccharide biosynthesis locus. Members of this family are generally found within a subcluster of seven or more genes including an epimerase/dehydratase, four genes homologous to the elements of the neuraminic (sialic) acid biosynthesis cluster (NeuABCD) and a nucleotidyl transferase. Together it is very likely that these enzymes direct the biosynthesis of a nine-carbon sugar analogous to CMP-neuraminic acid. These seven genes form the core of the cassette, although they are often accompanied by additional genes that may further modify the product sugar.
Pssm-ID: 275034 Cd Length: 359 Bit Score: 333.74 E-value: 1.69e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 28 PKLTDEEKQLVLDVLDSGrLVSSIGKYVKLFEEEFARYLGVRHAVATINGTASLHTAVASLNIGPGDEVITTPFSFIATA 107
Cdd:TIGR04181 6 PNFGGNEKKYVKECIDSG-WVSSVGAYVDRFEEKLAEYTGAKHAVAVVNGTAALHLALHLAGVKPGDEVITPALTFVATA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 108 TSILHNNAVPVFADIEKDSLNLDPATIEE---------------KITPR-TKAILVVHLAGYPAEMDEILKIAREHNLYV 171
Cdd:TIGR04181 85 NAISYLGAEPVFVDVDPDTLGLDPDALEEfleeeaerkdgvlinKETGRrIKACVPVHVFGHPADMDEIMEICDEWNLPV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 172 IEDCAQAIGSEYRGRKVGTFGDINAFSFYQTKNMTTGEGGMVTTDKEELYRYAKMFVDQGQES---KYYHTILGWNYRMT 248
Cdd:TIGR04181 165 VEDAAESLGSFYKGKHTGTFGDLGVFSFNGNKIITTGGGGMILTNDEELAKRAKHLSTTAKQPhpwEFEHDEVGYNYRMP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 249 ELQAALGLGQLRRIGELNAAREKIAQIYMDELSSLNG-DLLKLPvlkPYVKHTWHIFQVLLNLDKlrvNRDRIIEALKAE 327
Cdd:TIGR04181 245 NINAALGCAQLEQLEEFLARKRELAEIYKEFFSGIPGvEFLPEP---AGARSNYWLNALLLDSKL---DRDELLEALNEN 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 328 NVLVQVVYpRVIYENPLFQRltgygkgcpwlCPFYGkqitykkgsSPIAEQVARSVITLP 387
Cdd:TIGR04181 319 GIQTRPLW-TLMHELPMYRD-----------CPRDD---------LPVAENLEERLINLP 357
|
|
| PseC |
TIGR03588 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ... |
30-408 |
1.02e-110 |
|
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.
Pssm-ID: 274662 Cd Length: 380 Bit Score: 330.06 E-value: 1.02e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 30 LTDEEKQLVLDVLDSGRLVSsiGKYVKLFEEEFARYLGVRHAVATINGTASLHTAVASLNIGPGDEVITTPFSFIATATS 109
Cdd:TIGR03588 8 IDQDDIDAVVEVLKSDFLTQ--GPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFVATANC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 110 ILHNNAVPVFADIEKDSLNLDPATIEEKIT----PRTKAILVVHLAGYPAEMDEILKIAREHNLYVIEDCAQAIGSEYRG 185
Cdd:TIGR03588 86 ALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALGAEYGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 186 RKVGT--FGDINAFSFYQTKNMTTGEGGMVTTDKEELYRYAKMFVDQGQESK------------YYHTI-LGWNYRMTEL 250
Cdd:TIGR03588 166 KPVGNcrYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDpllfekqdegpwYYEQQeLGFNYRMTDI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 251 QAALGLGQLRRIGELNAAREKIAQIYMDELSSLngDLLKLPVLKPYVKHTWHIFQVLLNLDkLRVNRDRIIEALKAENVL 330
Cdd:TIGR03588 246 QAALGLSQLKKLDRFVAKRREIAARYDRLLKDL--PYFTPLTIPLGSKSAWHLYPILLDQE-FGCTRKEVFEALRAAGIG 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203628960 331 VQVVY-PrvIYENPLFQRLtgygkgcpwlcpfygkqitYKKGSSPIAEQVARSVITLPTLPGMTEEDAIDTANAIKKVL 408
Cdd:TIGR03588 323 VQVHYiP--VHLQPYYRQG-------------------FGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
|
|
| PRK11706 |
PRK11706 |
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional |
28-409 |
1.09e-86 |
|
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
Pssm-ID: 183283 Cd Length: 375 Bit Score: 268.24 E-value: 1.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 28 PKLTDEEKQLVLDVLDSGRLvSSIGKYVKLFEEEFARYLGVRHAVATINGTASLHTAVASLNIGPGDEVITTPFSFIATA 107
Cdd:PRK11706 7 PPVVGTELDYIQQAMSSGKL-CGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFVSTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 108 TSILHNNAVPVFADIEKDSLNLDPATIEEKITPRTKAILVVHLAGYPAEMDEILKIAREHNLYVIEDCAQAIGSEYRGRK 187
Cdd:PRK11706 86 NAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 188 VGTFGDINAFSFYQTKNMTTGEGGMVTTDKEELYRYA-----------KMFvdQGQESKYYHTILGWNYRMTELQAALGL 256
Cdd:PRK11706 166 LGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAeiirekgtnrsQFF--RGQVDKYTWVDIGSSYLPSELQAAYLW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 257 GQLRRIGELNAAREKIAQIYMDELSSL-NGDLLKLPVLKPYVKHTWHIFQVLLN-LDKlrvnRDRIIEALKAENVLVqvv 334
Cdd:PRK11706 244 AQLEAADRINQRRLALWQRYYDALAPLaEAGRIELPSIPDDCKHNAHMFYIKLRdLED----RSALINFLKEAGIMA--- 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203628960 335 yprVIYENPLFQrltgygkgCPwlcpfYGKQITYKKGSSPIAEQVARSVITLPTLPGMTEEDAIDTANAIKKVLT 409
Cdd:PRK11706 317 ---VFHYIPLHS--------SP-----AGERFGRFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEFFS 375
|
|
| PRK11658 |
PRK11658 |
UDP-4-amino-4-deoxy-L-arabinose aminotransferase; |
28-408 |
2.03e-81 |
|
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
Pssm-ID: 183263 Cd Length: 379 Bit Score: 254.95 E-value: 2.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 28 PKLTDEEKQLVLDVLDSGRLVSsiGKYVKLFEEEFARYLGVRHAVATINGTASLHTAVASLNIGPGDEVITTPFSFIATA 107
Cdd:PRK11658 10 PAMGDEELAAVKEVLRSGWITT--GPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 108 TSILHNNAVPVFADIEKDSLNLDPATIEEKITPRTKAILVVHLAGYPAEMDEILKIAREHNLYVIEDCAQAIGSEYRGRK 187
Cdd:PRK11658 88 NMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGRH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 188 VGTFGdiNA-FSFYQTKNMTTGEGGMVTTDKEELYRYAKMF------VD----QGQESKYYHTIL--GWNYRMTELQAAL 254
Cdd:PRK11658 168 IGARG--TAiFSFHAIKNITCAEGGLVVTDDDELADRLRSLkfhglgVDafdrQTQGRAPQAEVLtpGYKYNLADINAAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 255 GLGQLRRIGELNAAREKIAQIYMDELSSLNGDLLKLPVLKPyvKHTWHIFQVLLNLDKLRVNRDRIIEALKAENVlvqvv 334
Cdd:PRK11658 246 ALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPH--QHAWHLFIIRVDEERCGISRDALMEALKERGI----- 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203628960 335 yprviyenplfqrltgyGKGCPW----LCPFYGKQitYKKGSSPIAEQVARSVITLPTLPGMTEEDAIDTANAIKKVL 408
Cdd:PRK11658 319 -----------------GTGLHFraahTQKYYRER--FPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIA 377
|
|
| PRK15407 |
PRK15407 |
lipopolysaccharide biosynthesis protein RfbH; Provisional |
2-329 |
6.66e-72 |
|
lipopolysaccharide biosynthesis protein RfbH; Provisional
Pssm-ID: 237960 Cd Length: 438 Bit Score: 232.08 E-value: 6.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 2 FFSEVNMELPAIEGGKPVRPSFKEYfpklTDEEKQLVLD-VLDsGRLVSsiGKYVKLFEEEFARYLGVRHAVATINGTAS 80
Cdd:PRK15407 18 YAELAHAPKPFVPGKSPIPPSGKVI----DAKELQNLVDaSLD-FWLTT--GRFNDAFEKKLAEFLGVRYALLVNSGSSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 81 LHTAVASLN--------IGPGDEVITTPFSFIATATSILHNNAVPVFADIEKDSLNLDPATIEEKITPRTKAILVVHLAG 152
Cdd:PRK15407 91 NLLAFSALTspklgdraLKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 153 YPAEMDEILKIAREHNLYVIEDCAQAIGSEYRGRKVGTFGDINAFSFYQTKNMTTGEGGMVTTDKEELYRYAKMFVD--- 229
Cdd:PRK15407 171 NPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLKKIIESFRDwgr 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 230 ------------------------QGQESKYYHTILGWNYRMTELQAALGLGQLRRIGELNAAREKIAQIYMDELSSLnG 285
Cdd:PRK15407 251 dcwcapgcdntcgkrfgwqlgelpFGYDHKYTYSHLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASL-E 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2203628960 286 DLLKLPVLKPYVKHTWHIFQVLLNlDKLRVNRDRIIEALKAENV 329
Cdd:PRK15407 330 DFLILPEATPNSDPSWFGFPITVK-EDAGFTRVELVKYLEENKI 372
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
60-174 |
1.15e-14 |
|
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: 74.78 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 60 EEFARYLGVRHAVA--------TINGTASLHTAVASLnIGPGDEVI-TTPFsFIATATSILHNNAVPVFADI-EKDSLNL 129
Cdd:COG0436 74 EAIAAYYKRRYGVDldpdeilvTNGAKEALALALLAL-LNPGDEVLvPDPG-YPSYRAAVRLAGGKPVPVPLdEENGFLP 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2203628960 130 DPATIEEKITPRTKAILVVhlagYP----------AEMDEILKIAREHNLYVIED 174
Cdd:COG0436 152 DPEALEAAITPRTKAIVLN----SPnnptgavysrEELEALAELAREHDLLVISD 202
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
60-180 |
2.61e-13 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 70.94 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 60 EEFARYLGVRHA---VATINGTASLHTAVASL-NIGPGDEVITTPFSFiatatsilHNNAVP------------VFADIE 123
Cdd:COG0520 66 EKVARFIGAASPdeiIFTRGTTEAINLVAYGLgRLKPGDEILITEMEH--------HSNIVPwqelaertgaevRVIPLD 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203628960 124 kDSLNLDPATIEEKITPRTKAILVVHLA---GY--PAEmdEILKIAREHNLYVIEDCAQAIG 180
Cdd:COG0520 138 -EDGELDLEALEALLTPRTKLVAVTHVSnvtGTvnPVK--EIAALAHAHGALVLVDGAQSVP 196
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
60-174 |
1.44e-11 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 65.53 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 60 EEFARYLGVRHAVA---------TINGTASLHTAVASLnIGPGDEVITTPFSFIATA--TSILHNNAVPVFADIEKDsLN 128
Cdd:PRK07682 64 QEIAKYLKKRFAVSydpndeiivTVGASQALDVAMRAI-INPGDEVLIVEPSFVSYAplVTLAGGVPVPVATTLENE-FK 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203628960 129 LDPATIEEKITPRTKAILVVhlagYP----------AEMDEILKIAREHNLYVIED 174
Cdd:PRK07682 142 VQPAQIEAAITAKTKAILLC----SPnnptgavlnkSELEEIAVIVEKHDLIVLSD 193
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
86-174 |
6.04e-11 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 63.61 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 86 ASLNigPGDEV-ITTPfSFIATATSILHNNAVPVFADI-EKDSLNLDPATIEEKITPRTKAILVV-----HLAGY-PAEM 157
Cdd:PRK05764 110 ALLD--PGDEViIPAP-YWVSYPEMVKLAGGVPVFVPTgEENGFKLTVEQLEAAITPKTKALILNspsnpTGAVYsPEEL 186
|
90
....*....|....*..
gi 2203628960 158 DEILKIAREHNLYVIED 174
Cdd:PRK05764 187 EAIADVAVEHDIWVLSD 203
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
58-174 |
7.68e-11 |
|
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: 63.13 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 58 FEEEFARYLGVRHAVA--------TINGTASLHTAVASLnIGPGDEVITTPFSFIATATSILHNNAVPVFADI-EKDSLN 128
Cdd:cd00609 41 LREAIAEWLGRRGGVDvppeeivvTNGAQEALSLLLRAL-LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLdEEGGFL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203628960 129 LDPATIEEKITPRTKAILVVhlagYP----------AEMDEILKIAREHNLYVIED 174
Cdd:cd00609 120 LDLELLEAAKTPKTKLLYLN----NPnnptgavlseEELEELAELAKKHGILIISD 171
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
64-180 |
7.87e-10 |
|
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: 60.17 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 64 RYLGVRHAVA-------------TINGTASLHTAVASL--NIGPGDEVITT---------PFSFIATATsilhnNAVPVF 119
Cdd:cd06453 44 AYEAAREKVArfinapspdeiifTRNTTEAINLVAYGLgrANKPGDEIVTSvmehhsnivPWQQLAERT-----GAKLKV 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203628960 120 ADIEKDSlNLDPATIEEKITPRTKAILVVHLA---G--YPAEmdEILKIAREHNLYVIEDCAQAIG 180
Cdd:cd06453 119 VPVDDDG-QLDLEALEKLLTERTKLVAVTHVSnvlGtiNPVK--EIGEIAHEAGVPVLVDGAQSAG 181
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
63-174 |
4.32e-09 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 57.65 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 63 ARYLGVRHAVA--------TINGTASLHTAVASLnIGPGDEVIT-TP-FSFIATATSILHNNAVPVFADIEKDSLNLDPA 132
Cdd:PRK06108 71 ARYVSRLHGVAtpperiavTSSGVQALMLAAQAL-VGPGDEVVAvTPlWPNLVAAPKILGARVVCVPLDFGGGGWTLDLD 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2203628960 133 TIEEKITPRTKAILVVHLA---GYPAEMDE---ILKIAREHNLYVIED 174
Cdd:PRK06108 150 RLLAAITPRTRALFINSPNnptGWTASRDDlraILAHCRRHGLWIVAD 197
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
92-174 |
6.94e-09 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 57.17 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 92 PGDEVITT-PF-----SFiATATSIlhnNAVPVFADIEkDSLNLDP-ATIEEKITPRTKAILVVHLA---GY---PAEMD 158
Cdd:PRK07568 111 PGDEILVPePFyanynGF-ATSAGV---KIVPVTTKIE-EGFHLPSkEEIEKLITPKTKAILISNPGnptGVvytKEELE 185
|
90
....*....|....*.
gi 2203628960 159 EILKIAREHNLYVIED 174
Cdd:PRK07568 186 MLAEIAKKHDLFLISD 201
|
|
| PRK07550 |
PRK07550 |
aminotransferase; |
91-225 |
1.21e-08 |
|
aminotransferase;
Pssm-ID: 181026 [Multi-domain] Cd Length: 386 Bit Score: 56.51 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 91 GPGDEVI-TTPFSFI-ATATSILHNNAVPVFADiEKDSLNLDPATIEEKITPRTKAILVVHL-----AGYPAE-MDEILK 162
Cdd:PRK07550 112 GAGDEVIlPLPWYFNhKMWLDMLGIRPVYLPCD-EGPGLLPDPAAAEALITPRTRAIALVTPnnptgVVYPPElLHELYD 190
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203628960 163 IAREHNLYVIEDcaqaigSEYR------GRKVGTFGD-------INAFSFYQTKNMTTGEGGMVTTDKEELYRYAK 225
Cdd:PRK07550 191 LARRHGIALILD------ETYRdfdsggGAPHDLFADpdwddtlVHLYSFSKSYALTGHRVGAVVASPARIAEIEK 260
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
55-174 |
2.04e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 55.88 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 55 VKLFEEEFARYLGVRHAVATINGTASLHTAVASLnIGPGDEVITTPFSFIATATSILHNNAVPVFAD-IEKDSLNLDPAT 133
Cdd:PRK06348 76 IKYYSKNYDLSFKRNEIMATVGACHGMYLALQSI-LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKK 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2203628960 134 IEEKITPRTKAIlVVHLAGYPA-------EMDEILKIAREHNLYVIED 174
Cdd:PRK06348 155 LEALITSKTKAI-ILNSPNNPTgavfskeTLEEIAKIAIEYDLFIISD 201
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
58-216 |
1.06e-07 |
|
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: 51.23 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 58 FEEEFARYL--GVRHAVATINGTASLHTAVASLnIGPGDEVIttpfSFIATATSILHNNAVPVFADI------EKDSLNL 129
Cdd:cd01494 5 LEEKLARLLqpGNDKAVFVPSGTGANEAALLAL-LGPGDEVI----VDANGHGSRYWVAAELAGAKPvpvpvdDAGYGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 130 DPATIEEKITPRTKAILVVH----LAGYPAEMDEILKIAREHNLYVIEDCAQAIGSEYRGRKVGTFG--DINAFSFyqTK 203
Cdd:cd01494 80 DVAILEELKAKPNVALIVITpnttSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGgaDVVTFSL--HK 157
|
170
....*....|...
gi 2203628960 204 NMTTGEGGMVTTD 216
Cdd:cd01494 158 NLGGEGGGVVIVK 170
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
72-198 |
1.33e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 53.15 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 72 VATINGTASLHTAVASLnIGPGDEVI-TTPFSF-----IATAtsilhnNAVPVFADIEkDSLNLDPATIEEKITPRTKAI 145
Cdd:PRK05957 93 VVTAGSNMAFMNAILAI-TDPGDEIIlNTPYYFnhemaITMA------GCQPILVPTD-DNYQLQPEAIEQAITPKTRAI 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2203628960 146 LVVHL-----AGYP-AEMDEILKIAREHNLYVIEDCAQaigsEYRgrkvgTFGDINAFS 198
Cdd:PRK05957 165 VTISPnnptgVVYPeALLRAVNQICAEHGIYHISDEAY----EYF-----TYDGVKHFS 214
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
78-174 |
2.29e-07 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 52.50 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 78 TASLHTAVASLnIGPGDEVITTPFSFIATATSILHNNAVPVFAD-IEKDSLNLDPATIEEKITPRTKAILVVHL-----A 151
Cdd:PRK08363 103 TEALQLIFGAL-LDPGDEILIPGPSYPPYTGLVKFYGGVPVEYRtIEEEGWQPDIDDIRKKITEKTKAIAVINPnnptgA 181
|
90 100
....*....|....*....|....
gi 2203628960 152 GYPAE-MDEILKIAREHNLYVIED 174
Cdd:PRK08363 182 LYEKKtLKEILDIAGEHDLPVISD 205
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
58-176 |
2.46e-07 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 51.83 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 58 FEEEFARYLGVRHAVATINGTASLHTAVASLnIGPGDEVITTPFSFIATATS---ILHNNAVPVFADIEKDSlNLDPATI 134
Cdd:pfam01212 37 LEDRVAELFGKEAALFVPSGTAANQLALMAH-CQRGDEVICGEPAHIHFDETgghAELGGVQPRPLDGDEAG-NMDLEDL 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203628960 135 EEKIT-------PRTKAILV---VHLAG---YP-AEMDEILKIAREHNLYVIEDCA 176
Cdd:pfam01212 115 EAAIRevgadifPPTGLISLentHNSAGgqvVSlENLREIAALAREHGIPVHLDGA 170
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
11-176 |
2.56e-07 |
|
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: 51.87 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 11 PAIEGGKPVRPSFKEYFpkltdEEKQLVLDV-----LDSgrLVSSIGKYVKLfEEEFARYLGVRHAVATINGTASLHTAV 85
Cdd:cd00615 20 PGHKGGRGFRKSFYEFY-----GENLFKADVteltgLDD--LLDPTGPIKEA-QELAARAFGAKHTFFLVNGTSSSNKAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 86 ASLNIGPGDEVITTPFSFIATATSILHNNAVPVFADIEKDSLN-----LDPATIEEKIT--PRTKAILVVhlagYP---- 154
Cdd:cd00615 92 ILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYgiaggIPPETFKKALIehPDAKAAVIT----NPtyyg 167
|
170 180
....*....|....*....|....
gi 2203628960 155 --AEMDEILKIAREHNLYVIEDCA 176
Cdd:cd00615 168 icYNLRKIVEEAHHRGLPVLVDEA 191
|
|
| PRK09265 |
PRK09265 |
aminotransferase AlaT; Validated |
86-174 |
4.31e-07 |
|
aminotransferase AlaT; Validated
Pssm-ID: 181738 Cd Length: 404 Bit Score: 51.74 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 86 ASLNigPGDEV-ITTP-FSFIATATSILHNNAVPVFADiEKDSLNLDPATIEEKITPRTKAILVVHL-----AGYPAEM- 157
Cdd:PRK09265 114 ALLN--NGDEVlVPAPdYPLWTAAVSLSGGKPVHYLCD-EEAGWFPDLDDIRSKITPRTKAIVIINPnnptgAVYSKELl 190
|
90
....*....|....*..
gi 2203628960 158 DEILKIAREHNLYVIED 174
Cdd:PRK09265 191 EEIVEIARQHNLIIFAD 207
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
65-174 |
6.94e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 50.96 E-value: 6.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 65 YLGVRHAVA-TINGTASLHT----------AVASLNI------GPGDEVIT-TPFsFIATATSILHNNAVPVFADIEKDS 126
Cdd:PRK06836 75 YPEVREAIAeSLNRRFGTPLtadhivmtcgAAGALNValkailNPGDEVIVfAPY-FVEYRFYVDNHGGKLVVVPTDTDT 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203628960 127 LNLDPATIEEKITPRTKAIL---------VVhlagYPAE----MDEILKIARE---HNLYVIED 174
Cdd:PRK06836 154 FQPDLDALEAAITPKTKAVIinspnnptgVV----YSEEtlkaLAALLEEKSKeygRPIYLISD 213
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
59-181 |
3.93e-06 |
|
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: 48.40 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 59 EEEFARYLGVRHAVATI---NGTASLHTAVASL--NIGPGDEVITT---------PFSFIATATsilhnNAVPVFADIEK 124
Cdd:pfam00266 49 REKVAEFINAPSNDEIIftsGTTEAINLVALSLgrSLKPGDEIVITemehhanlvPWQELAKRT-----GARVRVLPLDE 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 125 DSLnLDPATIEEKITPRTKAILVVHLA---GYPAEMDEILKIAREHNLYVIEDCAQAIGS 181
Cdd:pfam00266 124 DGL-LDLDELEKLITPKTKLVAITHVSnvtGTIQPVPEIGKLAHQYGALVLVDAAQAIGH 182
|
|
| PRK07777 |
PRK07777 |
putative succinyldiaminopimelate transaminase DapC; |
74-174 |
1.43e-05 |
|
putative succinyldiaminopimelate transaminase DapC;
Pssm-ID: 236095 [Multi-domain] Cd Length: 387 Bit Score: 46.95 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 74 TINGTASLHTAVASLnIGPGDEVIT-TPF--SF---IATATSilHNNAVPVFADieKDSLNLDPATIEEKITPRTKAILV 147
Cdd:PRK07777 91 TVGATEAIAAAVLGL-VEPGDEVLLiEPYydSYaavIAMAGA--HRVPVPLVPD--GRGFALDLDALRAAVTPRTRALIV 165
|
90 100 110
....*....|....*....|....*....|...
gi 2203628960 148 --VH----LAGYPAEMDEILKIAREHNLYVIED 174
Cdd:PRK07777 166 nsPHnptgTVLTAAELAAIAELAVEHDLLVITD 198
|
|
| PRK13355 |
PRK13355 |
bifunctional HTH-domain containing protein/aminotransferase; Provisional |
123-174 |
2.35e-05 |
|
bifunctional HTH-domain containing protein/aminotransferase; Provisional
Pssm-ID: 237361 [Multi-domain] Cd Length: 517 Bit Score: 46.27 E-value: 2.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2203628960 123 EKDSLNLDPATIEEKITPRTKAILVVHL-----AGYPAE-MDEILKIAREHNLYVIED 174
Cdd:PRK13355 263 EQSEWYPDIDDIRSKITSRTKAIVIINPnnptgALYPREvLQQIVDIAREHQLIIFSD 320
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
69-179 |
6.90e-05 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 44.74 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 69 RHAVATINGTASLHTAVASL---NIGPGDEVITT---------PFSFIATATSilhnnAVPVFADIEKDSlNLDPATIEE 136
Cdd:PLN02855 95 REIVFTRNATEAINLVAYTWglaNLKPGDEVILSvaehhsnivPWQLVAQKTG-----AVLKFVGLTPDE-VLDVEQLKE 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2203628960 137 KITPRTKAILVVHLA---GYPAEMDEILKIAREHNLYVIEDCAQAI 179
Cdd:PLN02855 169 LLSEKTKLVATHHVSnvlGSILPVEDIVHWAHAVGAKVLVDACQSV 214
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
59-174 |
9.40e-05 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 44.32 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 59 EEEFARYLGVRHAVATINGTASLHTAVASLnIGPGDEVITTPFSFIATATSILHN------NAVpvFADIEkdslnlDPA 132
Cdd:PRK05994 69 EERVAALEGGTAALAVASGHAAQFLVFHTL-LQPGDEFIAARKLYGGSINQFGHAfksfgwQVR--WADAD------DPA 139
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2203628960 133 TIEEKITPRTKAILVVHLA---GYPAEMDEILKIAREHNLYVIED 174
Cdd:PRK05994 140 SFERAITPRTKAIFIESIAnpgGTVTDIAAIAEVAHRAGLPLIVD 184
|
|
| HisC |
COG0079 |
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ... |
63-172 |
1.18e-04 |
|
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]; Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 439849 [Multi-domain] Cd Length: 341 Bit Score: 43.97 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 63 ARYLGVRHA-VATINGTASLHTAVASLNIGPGDEVITTPFSFIATATSILHNNAVPVFADIEKDsLNLDPATIEEKITPR 141
Cdd:COG0079 58 AEYYGVPPEqVLVGNGSDELIQLLARAFLGPGDEVLVPEPTFSEYPIAARAAGAEVVEVPLDED-FSLDLDALLAAITER 136
|
90 100 110
....*....|....*....|....*....|....*....
gi 2203628960 142 TKAILVV--------HLAgyPAEMDEILKIAREHNLYVI 172
Cdd:COG0079 137 TDLVFLCnpnnptgtLLP--REELEALLEALPADGLVVV 173
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
60-174 |
1.76e-04 |
|
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: 43.66 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 60 EEFARYLGVRHAVAT------INGT-ASLHTAVASLnIGPGDEVIT---TPFSFIATATSiLHNNAVPVFADIEKdslnL 129
Cdd:COG1167 155 EAIARYLARRGVPASpdqiliTSGAqQALDLALRAL-LRPGDTVAVespTYPGALAALRA-AGLRLVPVPVDEDG----L 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203628960 130 DPATIEEKI-TPRTKAILVV---HlagYP--AEMD-----EILKIAREHNLYVIED 174
Cdd:COG1167 229 DLDALEAALrRHRPRAVYVTpshQ---NPtgATMSlerrrALLELARRHGVPIIED 281
|
|
| PRK12414 |
PRK12414 |
putative aminotransferase; Provisional |
60-147 |
2.10e-04 |
|
putative aminotransferase; Provisional
Pssm-ID: 183514 Cd Length: 384 Bit Score: 43.24 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 60 EEFARYLGVRHAVA---TINGTAS--LHTAVASLnIGPGDEVITTPFSFIATATSILHNNAVPVFADIEKDSLNLDPATI 134
Cdd:PRK12414 77 EKTERLYGARYDPAsevTVIASASegLYAAISAL-VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEV 155
|
90
....*....|...
gi 2203628960 135 EEKITPRTKAILV 147
Cdd:PRK12414 156 AAAITPRTRMIIV 168
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
62-174 |
3.70e-04 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 42.27 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 62 FARYLGV-----RHAVATINGTASLHTAVASLnIGPGDEVITTPFSFIATATSILHNNAVPVFADIEKDSLNLDPATIEE 136
Cdd:PRK08912 76 YARFQGLdldpeTEVMVTSGATEALAAALLAL-VEPGDEVVLFQPLYDAYLPLIRRAGGVPRLVRLEPPHWRLPRAALAA 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2203628960 137 KITPRTKAILV---VHLAGY---PAEMDEILKIAREHNLYVIED 174
Cdd:PRK08912 155 AFSPRTKAVLLnnpLNPAGKvfpREELALLAEFCQRHDAVAICD 198
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
55-174 |
4.80e-04 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 42.19 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 55 VKLFEEEFARYLGVRHAVATINGTASLHTAVASLNiGPGDEVITTPFSFIAT---ATSILHNNAVPV-FADIEkdslnlD 130
Cdd:cd00614 42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALL-KAGDHVVASDDLYGGTyrlFERLLPKLGIEVtFVDPD------D 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2203628960 131 PATIEEKITPRTKAILVVHLAGyP----AEMDEILKIAREHNLYVIED 174
Cdd:cd00614 115 PEALEAAIKPETKLVYVESPTN-PtlkvVDIEAIAELAHEHGALLVVD 161
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
74-174 |
5.56e-04 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 41.83 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 74 TINGTASLHTAVASLnIGPGDEVITTPFSFIATATSILHNNAVPVFADIEKDSLNLDPATIEEKITPRTKAILVvhlaGY 153
Cdd:PRK09082 97 TAGATEALFAAILAL-VRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLIIL----NT 171
|
90 100 110
....*....|....*....|....*....|.
gi 2203628960 154 P----------AEMDEILKIAREHNLYVIED 174
Cdd:PRK09082 172 PhnpsgtvwsaADMRALWQLIAGTDIYVLSD 202
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
58-180 |
1.76e-03 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 40.37 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 58 FEEEFARYLGVRH--------AVATINGTASLHTAVASLNIGPGDEVITTPFSFIATATSILHNNAVPV-FADIEKDSLN 128
Cdd:pfam00155 44 LREALAKFLGRSPvlkldreaAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVrYPLYDSNDFH 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2203628960 129 LDPATIEEKITPRTKAILV--VH----LAGYPAEMDEILKIAREHNLYVIEDCAQAIG 180
Cdd:pfam00155 124 LDFDALEAALKEKPKVVLHtsPHnptgTVATLEELEKLLDLAKEHNILLLVDEAYAGF 181
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
53-171 |
3.17e-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: 39.24 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 53 KYVKLFEEEFARYLGVRHAVATINGTASLHTAVASLnIGPGDEVITTPFSFIAT---ATSILHNNAVPVFADIEKDSLnl 129
Cdd:cd06502 32 PTTAKLEARAAELFGKEAALFVPSGTAANQLALAAH-TQPGGSVICHETAHIYTdeaGAPEFLSGVKLLPVPGENGKL-- 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2203628960 130 DPATIEEKIT-------PRTKAILV---VHLAGY--PAEMDEILKIAREHNLYV 171
Cdd:cd06502 109 TPEDLEAAIRprddihfPPPSLVSLentTEGGTVypLDELKAISALAKENGLPL 162
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
112-174 |
4.31e-03 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 38.92 E-value: 4.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203628960 112 HNNAVPVFADIEkdslnlDPATIEEKITPRTKAILvVHLAGYP----AEMDEILKIAREHNLYVIED 174
Cdd:PRK08247 113 KWNVRFVYVNTA------SLKAIEQAITPNTKAIF-IETPTNPlmqeTDIAAIAKIAKKHGLLLIVD 172
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
92-174 |
5.65e-03 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 38.55 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203628960 92 PGDEVITTPFSFIATATSILHNNAVPVFADIEKDSLNLDPATIEEKITPRTKAILVvhlaGYPA----------EMDEIL 161
Cdd:PRK07683 112 PGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVL----PYPSnptgvtlskeELQDIA 187
|
90
....*....|...
gi 2203628960 162 KIAREHNLYVIED 174
Cdd:PRK07683 188 DVLKDKNIFVLSD 200
|
|
| |
