|
Name |
Accession |
Description |
Interval |
E-value |
| Bna5 |
COG3844 |
Kynureninase [Amino acid transport and metabolism]; |
1-416 |
0e+00 |
|
Kynureninase [Amino acid transport and metabolism];
Pssm-ID: 443054 [Multi-domain] Cd Length: 420 Bit Score: 692.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 1 MTTRDDCLALDAGDPLADLRQLFALPD-GVIYLDGNSLGARPRAAVERAAEVVAAEWGEGLIRSWNSADWRGLPERLGDK 79
Cdd:COG3844 2 ETTRAFARALDAADPLAAFRDRFHLPDdGVIYLDGNSLGLLPKAAAARLAEVLEEEWGELLIRGWNEAPWFDLPERLGDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 80 LAPLIGARAGEVVITDTTSINLFKVLSAALRIQeedaPGRKVIVSESSNFPTDLYIAEGLTDMLQRGYRLRLVD------ 153
Cdd:COG3844 82 LARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPR----PGRTKILSEADNFPTDRYALEGQARLHGLDEELRLVEprdget 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 154 -DPEQLPAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTYKYLNGG 232
Cdd:COG3844 158 lRPEDIEAALDDDVALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHSAGAVPVDLHDWGVDFAVGCTYKYLNGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 233 PGSPAYVWVAPRLRERVWQPLSGWFGHSRQFAMEPRYQPGEGITRFLCGTQPITSLALVECGLDIFARTDMQRLRDKSLA 312
Cdd:COG3844 238 PGAPAFLYVHERHQDRLLQPLAGWWGHATPFAMEPGYEPAPGARRFQLGTPPILSMAALEASLDLFEEAGMDALRAKSLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 313 LADLFIELVESRCERFGLTLVTPREHARRGSHVSFEHAQGYAIVQALIDRGVIGDYREPGILRFGFTPLYTRFVEVWDAV 392
Cdd:COG3844 318 LTDYLIFLVEERLAPLGLELITPRDPARRGSQVSLRHPEAYAIFQALIERGVIGDFREPDVIRFGPTPLYTSFEDVWRAV 397
|
410 420
....*....|....*....|....
gi 15597276 393 QALLEILQSEAWKEPRyQVRHKVT 416
Cdd:COG3844 398 EILREILEEGEWEKFE-NERGAVT 420
|
|
| kynureninase |
TIGR01814 |
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ... |
7-399 |
1.85e-154 |
|
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130873 [Multi-domain] Cd Length: 406 Bit Score: 442.64 E-value: 1.85e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 7 CLALDAGDPLADLRQLFALP-----DGVIYLDGNSLGARPRAAvERAAEVVAAEWGEGLIRSWNSAD--WRGLPERLGDK 79
Cdd:TIGR01814 1 ALELDEADPLRALRDEFHLPkigdeNAVIYLDGNSLGLMPKAA-RNALKEELDKWAKIAIRGHNTGKapWFTLDESLLKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 80 LAplIGARAGEVVITDTTSINLFKVLSAALRIQEEdapgRKVIVSESSNFPTDLYIAE------GLTD---MLQ----RG 146
Cdd:TIGR01814 80 RL--VGAKEDEVVVMNTLTINLHLLLASFYKPTPK----RYKILLEAKAFPSDHYAIEsqlqlhGLTVeesMVQieprEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 147 YRLRLVDDPEQLpAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTY 226
Cdd:TIGR01814 154 ETLRLEDILDTI-EKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDFACWCTY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 227 KYLNGGPGSPAYVWVAPRLRERVWQPlsGWFGHSR--QFAMEPRYQPgEGITRFLCgTQPITSLALVECGLDIFARTDMQ 304
Cdd:TIGR01814 233 KYLNAGPGAGAFVHEKHAHTERPRLA--GWWGHARptRFKMDNTLGL-IPCGFRIS-NPPILSVAALRGSLDIFDQAGME 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 305 RLRDKSLALADLFIELVESRC-ERFGLTLVTPREHARRGSHVSFEHA-QGYAIVQALIDRGVIGDYREPGILRFGFTPLY 382
Cdd:TIGR01814 309 ALRKKSLLLTDYLEELIKARCgGPPVLTIITPRDHAQRGCQLSLTHPvPGKAVFQALIKRGVIGDKREPSVIRVAPVPLY 388
|
410
....*....|....*..
gi 15597276 383 TRFVEVWDAVQALLEIL 399
Cdd:TIGR01814 389 NTFVDVYDAVNVLEEIL 405
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
30-364 |
1.42e-17 |
|
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: 83.45 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 30 IYLDGNSLGARPRAAVERAAEvvaaewgegLIRSWNSADWRGLPERLGD----------KLAPLIGARAG-EVVITD--T 96
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQE---------YYTDYNGNVHRGVHTLGKEatqayeeareKVAEFINAPSNdEIIFTSgtT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 97 TSINLFkVLSAALRIQeedaPGRKVIVSES---SNFPTDLYIAEgltdmlQRGYRLRLVD-------DPEQLPAAIDADT 166
Cdd:pfam00266 72 EAINLV-ALSLGRSLK----PGDEIVITEMehhANLVPWQELAK------RTGARVRVLPldedgllDLDELEKLITPKT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 167 AVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADAD-YAIGcTYKyLNGGPGSPAyVWVAPRL 245
Cdd:pfam00266 141 KLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDfLAFS-GHK-LYGPTGIGV-LYGRRDL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 246 RERvWQPLSGWfGHSRQFAMEPRYQPGEGITRFLCGTQPITSLALVECGLDIFARTDMQRLRDKSLALADLFIELVESR- 324
Cdd:pfam00266 218 LEK-MPPLLGG-GGMIETVSLQESTFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLp 295
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15597276 325 -CERFGltlvtpreHARRGSHVSFEHAQ--GYAIVQALIDRGV 364
Cdd:pfam00266 296 gIRLYG--------PERRASIISFNFKGvhPHDVATLLDESGI 330
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
78-364 |
2.50e-14 |
|
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: 74.04 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 78 DKLAPLIGAR-AGEVVITD--TTSINLfkVLSAALRIQEedaPGRKVIVSES---SNFPTDLYIAEgltdmlQRGYRLRL 151
Cdd:cd06453 50 EKVARFINAPsPDEIIFTRntTEAINL--VAYGLGRANK---PGDEIVTSVMehhSNIVPWQQLAE------RTGAKLKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 152 VD-------DPEQLPAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADAD-YAI- 222
Cdd:cd06453 119 VPvdddgqlDLEALEKLLTERTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDfLAFs 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 223 GctYKYLnGGPGSPAyVWVAPRLRERVWQPLSGwfGHSRQFAMEPRYQPGEGITRFLCGTQPIT-SLALVEcGLDIFART 301
Cdd:cd06453 199 G--HKML-GPTGIGV-LYGKEELLEEMPPYGGG--GEMIEEVSFEETTYADLPHKFEAGTPNIAgAIGLGA-AIDYLEKI 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597276 302 DMQRLRDKSLALADLFIELVesrCERFGLTLVTPREHarRGSHVSFE----HAqgYAIVQALIDRGV 364
Cdd:cd06453 272 GMEAIAAHEHELTAYALERL---SEIPGVRVYGDAED--RAGVVSFNlegiHP--HDVATILDQYGI 331
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
17-221 |
2.35e-11 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 65.06 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 17 ADLRQLF-ALPDGVIYLDGNSLGARPRAAVERAAEVVAAEWGEgLIRSWNSADWRgLPERLG---DKLAPLIGARAGEVV 92
Cdd:PRK10874 7 AQFRAQFpALQDAGVYLDSAATALKPQAVIEATQQFYSLSAGN-VHRSQFAAAQR-LTARYEaarEQVAQLLNAPDAKNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 93 I---TDTTSINLFKVLSAALRIQeedaPGRKVIVSES---SNFPTDLYIAEgltdmlQRGYRL-------RLVDDPEQLP 159
Cdd:PRK10874 85 VwtrGTTESINLVAQSYARPRLQ----PGDEIIVSEAehhANLVPWLMVAQ------QTGAKVvklplgaDRLPDVDLLP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597276 160 AAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADAD-YA 221
Cdd:PRK10874 155 ELITPRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDfYA 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Bna5 |
COG3844 |
Kynureninase [Amino acid transport and metabolism]; |
1-416 |
0e+00 |
|
Kynureninase [Amino acid transport and metabolism];
Pssm-ID: 443054 [Multi-domain] Cd Length: 420 Bit Score: 692.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 1 MTTRDDCLALDAGDPLADLRQLFALPD-GVIYLDGNSLGARPRAAVERAAEVVAAEWGEGLIRSWNSADWRGLPERLGDK 79
Cdd:COG3844 2 ETTRAFARALDAADPLAAFRDRFHLPDdGVIYLDGNSLGLLPKAAAARLAEVLEEEWGELLIRGWNEAPWFDLPERLGDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 80 LAPLIGARAGEVVITDTTSINLFKVLSAALRIQeedaPGRKVIVSESSNFPTDLYIAEGLTDMLQRGYRLRLVD------ 153
Cdd:COG3844 82 LARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPR----PGRTKILSEADNFPTDRYALEGQARLHGLDEELRLVEprdget 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 154 -DPEQLPAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTYKYLNGG 232
Cdd:COG3844 158 lRPEDIEAALDDDVALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHSAGAVPVDLHDWGVDFAVGCTYKYLNGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 233 PGSPAYVWVAPRLRERVWQPLSGWFGHSRQFAMEPRYQPGEGITRFLCGTQPITSLALVECGLDIFARTDMQRLRDKSLA 312
Cdd:COG3844 238 PGAPAFLYVHERHQDRLLQPLAGWWGHATPFAMEPGYEPAPGARRFQLGTPPILSMAALEASLDLFEEAGMDALRAKSLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 313 LADLFIELVESRCERFGLTLVTPREHARRGSHVSFEHAQGYAIVQALIDRGVIGDYREPGILRFGFTPLYTRFVEVWDAV 392
Cdd:COG3844 318 LTDYLIFLVEERLAPLGLELITPRDPARRGSQVSLRHPEAYAIFQALIERGVIGDFREPDVIRFGPTPLYTSFEDVWRAV 397
|
410 420
....*....|....*....|....
gi 15597276 393 QALLEILQSEAWKEPRyQVRHKVT 416
Cdd:COG3844 398 EILREILEEGEWEKFE-NERGAVT 420
|
|
| kynureninase |
TIGR01814 |
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ... |
7-399 |
1.85e-154 |
|
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130873 [Multi-domain] Cd Length: 406 Bit Score: 442.64 E-value: 1.85e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 7 CLALDAGDPLADLRQLFALP-----DGVIYLDGNSLGARPRAAvERAAEVVAAEWGEGLIRSWNSAD--WRGLPERLGDK 79
Cdd:TIGR01814 1 ALELDEADPLRALRDEFHLPkigdeNAVIYLDGNSLGLMPKAA-RNALKEELDKWAKIAIRGHNTGKapWFTLDESLLKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 80 LAplIGARAGEVVITDTTSINLFKVLSAALRIQEEdapgRKVIVSESSNFPTDLYIAE------GLTD---MLQ----RG 146
Cdd:TIGR01814 80 RL--VGAKEDEVVVMNTLTINLHLLLASFYKPTPK----RYKILLEAKAFPSDHYAIEsqlqlhGLTVeesMVQieprEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 147 YRLRLVDDPEQLpAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTY 226
Cdd:TIGR01814 154 ETLRLEDILDTI-EKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDFACWCTY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 227 KYLNGGPGSPAYVWVAPRLRERVWQPlsGWFGHSR--QFAMEPRYQPgEGITRFLCgTQPITSLALVECGLDIFARTDMQ 304
Cdd:TIGR01814 233 KYLNAGPGAGAFVHEKHAHTERPRLA--GWWGHARptRFKMDNTLGL-IPCGFRIS-NPPILSVAALRGSLDIFDQAGME 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 305 RLRDKSLALADLFIELVESRC-ERFGLTLVTPREHARRGSHVSFEHA-QGYAIVQALIDRGVIGDYREPGILRFGFTPLY 382
Cdd:TIGR01814 309 ALRKKSLLLTDYLEELIKARCgGPPVLTIITPRDHAQRGCQLSLTHPvPGKAVFQALIKRGVIGDKREPSVIRVAPVPLY 388
|
410
....*....|....*..
gi 15597276 383 TRFVEVWDAVQALLEIL 399
Cdd:TIGR01814 389 NTFVDVYDAVNVLEEIL 405
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
16-364 |
5.48e-29 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 116.78 E-value: 5.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 16 LADLRQLF-ALPDGVIYLDGNSLGARPRAAVERAAEVVAAEWGEGLIRSWNSADWR-GLPERLGDKLAPLIGAR-AGEVV 92
Cdd:COG0520 2 VEAIRADFpVLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEAtDAYEAAREKVARFIGAAsPDEII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 93 ITD--TTSINLfkVLSAALRIQeedaPGRKVIVSES---SNFPTDLYIAEgltdmlQRGYRLRLVD-------DPEQLPA 160
Cdd:COG0520 82 FTRgtTEAINL--VAYGLGRLK----PGDEILITEMehhSNIVPWQELAE------RTGAEVRVIPldedgelDLEALEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 161 AIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTYKYlnGGPGSPAYVW 240
Cdd:COG0520 150 LLTPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKL--YGPTGIGVLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 241 VAPRLRERVWQPLSGwfGHSRQFAMEPRYQPGEGITRFLCGTQPI-TSLALVECgLDIFARTDMQRLRDKSLALADLFIE 319
Cdd:COG0520 228 GKRELLEALPPFLGG--GGMIEWVSFDGTTYADLPRRFEAGTPNIaGAIGLGAA-IDYLEAIGMEAIEARERELTAYALE 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15597276 320 LVEsrcERFGLTLVTPREHARRGSHVSF--EHAQGYAIVQALIDRGV 364
Cdd:COG0520 305 GLA---AIPGVRILGPADPEDRSGIVSFnvDGVHPHDVAALLDDEGI 348
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
30-364 |
1.42e-17 |
|
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: 83.45 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 30 IYLDGNSLGARPRAAVERAAEvvaaewgegLIRSWNSADWRGLPERLGD----------KLAPLIGARAG-EVVITD--T 96
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQE---------YYTDYNGNVHRGVHTLGKEatqayeeareKVAEFINAPSNdEIIFTSgtT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 97 TSINLFkVLSAALRIQeedaPGRKVIVSES---SNFPTDLYIAEgltdmlQRGYRLRLVD-------DPEQLPAAIDADT 166
Cdd:pfam00266 72 EAINLV-ALSLGRSLK----PGDEIVITEMehhANLVPWQELAK------RTGARVRVLPldedgllDLDELEKLITPKT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 167 AVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADAD-YAIGcTYKyLNGGPGSPAyVWVAPRL 245
Cdd:pfam00266 141 KLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDfLAFS-GHK-LYGPTGIGV-LYGRRDL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 246 RERvWQPLSGWfGHSRQFAMEPRYQPGEGITRFLCGTQPITSLALVECGLDIFARTDMQRLRDKSLALADLFIELVESR- 324
Cdd:pfam00266 218 LEK-MPPLLGG-GGMIETVSLQESTFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLp 295
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15597276 325 -CERFGltlvtpreHARRGSHVSFEHAQ--GYAIVQALIDRGV 364
Cdd:pfam00266 296 gIRLYG--------PERRASIISFNFKGvhPHDVATLLDESGI 330
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
78-364 |
2.50e-14 |
|
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: 74.04 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 78 DKLAPLIGAR-AGEVVITD--TTSINLfkVLSAALRIQEedaPGRKVIVSES---SNFPTDLYIAEgltdmlQRGYRLRL 151
Cdd:cd06453 50 EKVARFINAPsPDEIIFTRntTEAINL--VAYGLGRANK---PGDEIVTSVMehhSNIVPWQQLAE------RTGAKLKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 152 VD-------DPEQLPAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADAD-YAI- 222
Cdd:cd06453 119 VPvdddgqlDLEALEKLLTERTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDfLAFs 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 223 GctYKYLnGGPGSPAyVWVAPRLRERVWQPLSGwfGHSRQFAMEPRYQPGEGITRFLCGTQPIT-SLALVEcGLDIFART 301
Cdd:cd06453 199 G--HKML-GPTGIGV-LYGKEELLEEMPPYGGG--GEMIEEVSFEETTYADLPHKFEAGTPNIAgAIGLGA-AIDYLEKI 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597276 302 DMQRLRDKSLALADLFIELVesrCERFGLTLVTPREHarRGSHVSFE----HAqgYAIVQALIDRGV 364
Cdd:cd06453 272 GMEAIAAHEHELTAYALERL---SEIPGVRVYGDAED--RAGVVSFNlegiHP--HDVATILDQYGI 331
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
17-221 |
2.35e-11 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 65.06 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 17 ADLRQLF-ALPDGVIYLDGNSLGARPRAAVERAAEVVAAEWGEgLIRSWNSADWRgLPERLG---DKLAPLIGARAGEVV 92
Cdd:PRK10874 7 AQFRAQFpALQDAGVYLDSAATALKPQAVIEATQQFYSLSAGN-VHRSQFAAAQR-LTARYEaarEQVAQLLNAPDAKNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 93 I---TDTTSINLFKVLSAALRIQeedaPGRKVIVSES---SNFPTDLYIAEgltdmlQRGYRL-------RLVDDPEQLP 159
Cdd:PRK10874 85 VwtrGTTESINLVAQSYARPRLQ----PGDEIIVSEAehhANLVPWLMVAQ------QTGAKVvklplgaDRLPDVDLLP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597276 160 AAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADAD-YA 221
Cdd:PRK10874 155 ELITPRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDfYA 217
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
79-359 |
7.39e-11 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 63.13 E-value: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 79 KLAPLIGARAGEVVITD--TTSINLfkVLSAALRIQEEDapgRKVIVSESSNFPTdlyIAEGLTDMLQRGYRLRLVD--- 153
Cdd:PLN02651 51 QVAALIGADPKEIIFTSgaTESNNL--AIKGVMHFYKDK---KKHVITTQTEHKC---VLDSCRHLQQEGFEVTYLPvks 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 154 ----DPEQLPAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTYKYl 229
Cdd:PLN02651 123 dglvDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKI- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 230 nGGPGSPAYVWVAPRLRERVWQPLSGWfGHSRqfamepryqpgeGITrflCGTQPITslaLV-----ECGLdifARTDMQ 304
Cdd:PLN02651 202 -YGPKGVGALYVRRRPRVRLEPLMSGG-GQER------------GRR---SGTENTP---LVvglgaACEL---AMKEMD 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597276 305 RLRDKSLALADLFIELVESRCErfGLTLVTPREHARR--GS-HVSFEHAQGYAIVQAL 359
Cdd:PLN02651 259 YDEKHMKALRERLLNGLRAKLG--GVRVNGPRDPEKRypGTlNLSFAYVEGESLLMGL 314
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
117-248 |
6.75e-08 |
|
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: 53.83 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 117 PGRKVIVSESSNFptdlyiAEGLTDMLQR-GYRLRLVD-------DPEQLPAAIDADTA-VVMLSHVNYKTGYLHDMREV 187
Cdd:cd06451 73 PGDKVLVGVNGVF------GDRWADMAERyGADVDVVEkpwgeavSPEEIAEALEQHDIkAVTLTHNETSTGVLNPLEGI 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597276 188 TRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTYKYLNGGPGSpAYVWVAPRLRER 248
Cdd:cd06451 147 GALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGL-GPIAFSERALER 206
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
152-199 |
1.16e-05 |
|
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440172 [Multi-domain] Cd Length: 442 Bit Score: 47.33 E-value: 1.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15597276 152 VDDPEQLPAAIDADTAVVMLSHVNYkTGYLHDMREVTRLVHENGALAI 199
Cdd:COG0403 192 VTDLEALKALLDDDVAGVLVQYPNF-FGVIEDLRAIAEAAHAAGALVI 238
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
30-240 |
1.71e-05 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 46.66 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 30 IYLDGNSLGARPRAAVERAAEVVaaewgegliRSWNSADWRGLP----------ERLGDKLAPLIGARA-GEVVITD--T 96
Cdd:PLN02855 34 VYLDNAATSQKPAAVLDALQDYY---------EEYNSNVHRGIHalsakatdayELARKKVAAFINASTsREIVFTRnaT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 97 TSINLFKVLSAALRIQeedaPGRKVIVSES---SNF-PTDLyIAEgltdmlQRGYRLRLVD-------DPEQLPAAIDAD 165
Cdd:PLN02855 105 EAINLVAYTWGLANLK----PGDEVILSVAehhSNIvPWQL-VAQ------KTGAVLKFVGltpdevlDVEQLKELLSEK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597276 166 TAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTYKYLngGPGSPAYVW 240
Cdd:PLN02855 174 TKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMC--GPTGIGFLW 246
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
147-239 |
3.22e-05 |
|
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: 44.30 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 147 YRLRLVDDPEQLPAAIdadTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTY 226
Cdd:cd01494 77 GGLDVAILEELKAKPN---VALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTF 153
|
90
....*....|....*.
gi 15597276 227 ---KYLNGGPGSPAYV 239
Cdd:cd01494 154 slhKNLGGEGGGVVIV 169
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
167-227 |
3.70e-05 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 45.46 E-value: 3.70e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597276 167 AVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTYK 227
Cdd:cd06452 141 ALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHK 201
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
154-227 |
4.42e-05 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 45.31 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 154 DPEQLPAAIDA-------DTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTY 226
Cdd:PRK09331 140 TPEAYAEKIEEvkeetgkPPALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGH 219
|
.
gi 15597276 227 K 227
Cdd:PRK09331 220 K 220
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
152-199 |
7.39e-05 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 44.74 E-value: 7.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15597276 152 VDDPEQLPAAIDADTAVVMLSHVNYkTGYLHDMREVTRLVHENGALAI 199
Cdd:PRK00451 191 VTDLEALEAAVDDDTAAVVVQYPNF-FGVIEDLEEIAEIAHAGGALFI 237
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
146-231 |
3.07e-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: 42.57 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 146 GYRLRLVD--DPEQLPAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWD--LAHSAGALPLDLhaaDADYA 221
Cdd:cd00614 104 GIEVTFVDpdDPEALEAAIKPETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDntFATPYLQRPLEL---GADIV 180
|
90
....*....|
gi 15597276 222 IGCTYKYLNG 231
Cdd:cd00614 181 VHSATKYIGG 190
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
143-208 |
1.42e-03 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 40.44 E-value: 1.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597276 143 LQRGYRLRLVD--------DPEQLPAAIDADTAVVMLSHVNyktGYLHDMREVTRLVHENGALAIWDLAHSAGA 208
Cdd:COG0399 88 LYVGATPVFVDidpdtyniDPEALEAAITPRTKAIIPVHLY---GQPADMDAIMAIAKKHGLKVIEDAAQALGA 158
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
156-253 |
2.94e-03 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 39.71 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 156 EQLPAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHENGALAIWDLAHSAGALPLDLHAADADYAIGCTYK-YlngGPG 234
Cdd:PRK02948 129 VDLERAITPDTVLASIQHANSEIGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKiY---GPK 205
|
90
....*....|....*....
gi 15597276 235 SPAYVWVAPRLRervWQPL 253
Cdd:PRK02948 206 GVGAVYINPQVR---WKPV 221
|
|
| PRK06234 |
PRK06234 |
methionine gamma-lyase; Provisional |
78-231 |
6.55e-03 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 168478 [Multi-domain] Cd Length: 400 Bit Score: 38.65 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 78 DKLAPLIGARAGEVVITDTTSIN--LFKVLSAalriqeedapGRKVIVSESSNFPTDLYIAEGLTDMlqrGYRLRLVD-- 153
Cdd:PRK06234 71 NKLALLEGGEAAVVAASGMGAISssLWSALKA----------GDHVVASDTLYGCTFALLNHGLTRY---GVEVTFVDts 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 154 DPEQLPAAIDADTAVVMLSHVNYKTGYLHDMREVTRLVHEN--GALAIWDLAHSAGAL--PLDLhaaDADYAIGCTYKYL 229
Cdd:PRK06234 138 NLEEVRNALKANTKVVYLETPANPTLKVTDIKAISNIAHENnkECLVFVDNTFCTPYIqrPLQL---GADVVVHSATKYL 214
|
..
gi 15597276 230 NG 231
Cdd:PRK06234 215 NG 216
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
108-208 |
7.14e-03 |
|
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: 38.29 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597276 108 ALRIQeedaPGRKVIVSESSNFPTdlyiAEGLtdmLQRGYRLRLVD--------DPEQLPAAIDADTAVVMLSHVnykTG 179
Cdd:cd00616 52 ALGIG----PGDEVIVPSFTFVAT----ANAI---LLLGATPVFVDidpdtyniDPELIEAAITPRTKAIIPVHL---YG 117
|
90 100
....*....|....*....|....*....
gi 15597276 180 YLHDMREVTRLVHENGALAIWDLAHSAGA 208
Cdd:cd00616 118 NPADMDAIMAIAKRHGLPVIEDAAQALGA 146
|
|
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
154-201 |
7.65e-03 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 38.55 E-value: 7.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15597276 154 DPEQLPAAIDADTAVVMLSHVNyKTG-YLHDMREVTRLVHENGALAIWD 201
Cdd:PRK04366 197 DLEALKAAVGEDTAALMLTNPN-TLGlFERNILEIAEIVHEAGGLLYYD 244
|
|
| |
