|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
7-483 |
0e+00 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 908.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 7 PLIFERSREGRYAYSLPKSDIKTnSVESLLDDKFIRKNKAEFPEVAELDLVRHYTELSNKNFGVDNGFYPLGSCTMKYNP 86
Cdd:PRK04366 6 PLIFELSRPGRRGYSLPELDVPE-VLESLLPEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDTGFYPLGSCTMKYNP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 87 KINEKVARIPGFSESHPLQDEDQVQGSLEIIYSLQEELKEITGMDEVTLQPAAGAHGEWTALMIFKAYHENNGEGHRDEV 166
Cdd:PRK04366 85 KINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAHGELTGLLMIRAYHEARGDTKRTEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 167 IVPDSAHGTNPASASFAGFKSVTVKSNERGEVDIDDLKRVVNENTAAIMLTNPNTLGIFEKNIMEIREIVHNAGGLLYYD 246
Cdd:PRK04366 165 IVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTAALMLTNPNTLGLFERNILEIAEIVHEAGGLLYYD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 247 GANLNAIMDKVRPGDMGFDAVHLNLHKTFTgphggggpgsgpvgvvKELASYLPKPMVIKDGDKFKYDNDIKNSIGRVKP 326
Cdd:PRK04366 245 GANLNAILGKARPGDMGFDVVHLNLHKTFStphggggpgsgpvgvkEELAPFLPVPVVEKDGDRYRLDYDRPKSIGRVRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 327 FYGNFGIYLRAYTYIRTMGATGLKEVSEAAVLNANYIKARLSEHFEIPYKQYCKHEFVLSGVRQKEFGVRTLDMAKRLLD 406
Cdd:PRK04366 325 FYGNFGVLVRAYAYIRSLGAEGLREVSEDAVLNANYLKARLKDIYDLPYDRPCMHEFVLSGKKLKETGVRTLDIAKRLLD 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581145584 407 FGVHPPTIYFPLNVEEGMMIEPTETESKETLDYFIDTLISIAEEAKNDPDKVLEAPHTTVIDRLDEATAARKPILKF 483
Cdd:PRK04366 405 YGFHPPTIYFPLIVPEALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLDEVKAARKPVLRW 481
|
|
| GcvP2 |
COG1003 |
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ... |
20-484 |
0e+00 |
|
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440627 Cd Length: 468 Bit Score: 808.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 20 YSLPKSDIktnSVESLLDDKFIRKNKAEFPEVAELDLVRHYTELSNKNFGVDNGFYPLGSCTMKYNPKINEKVARIPGFS 99
Cdd:COG1003 1 VSLPEPEA---DAASLLPEALLRKSPVFLPEVSETEVLRHYTRLSQKNLGLDTGMIPLGSCTMKYNPKINEEPATLPGFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 100 ESHPLQDEDQVQGSLEIIYSLQEELKEITGMDEVTLQPAAGAHGEWTALMIFKAYHENNGEGHRDEVIVPDSAHGTNPAS 179
Cdd:COG1003 78 NLHPFQPEETVQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGEGHRNEILIPDSAHGTNPAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 180 ASFAGFKSVTVKSNERGEVDIDDLKRVVNENTAAIMLTNPNTLGIFEKNIMEIREIVHNAGGLLYYDGANLNAIMDKVRP 259
Cdd:COG1003 158 AAMAGFKVVVVKSDEDGNVDLEDLKAKVGDRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 260 GDMGFDAVHLNLHKTFTgphggggpgsgpvgvvKELASYLPKPMVIKDGDKFKYDNDIKNSIGRVKPFYGNFGIYLRAYT 339
Cdd:COG1003 238 GDMGFDVCHLNLHKTFStphggggpgsgpvgvkEHLAPFLPGPPVVKDGDKYRLDYDRPKSIGRSAAFYGNAGVLVRAYA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 340 YIRTMGATGLKEVSEAAVLNANYIKARLSEHFEIPYK--QYCKHEFVLSGVRQK-EFGVRTLDMAKRLLDFGVHPPTIYF 416
Cdd:COG1003 318 YIRMMGAEGLREATEVAVLNANYLAARLKDHYPVLYTgnGRCAHEFILDLRPLKkETGVTTLDIAKRLLDYGFHAPTMYF 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581145584 417 PLNVEEGMMIEPTETESKETLDYFIDTLISIAEEAKNDPDKVLEAPHTTVIDRLDEATAARKPILKFE 484
Cdd:COG1003 398 PLIVPETLMIEPTESESKEELDRFIDAMIAIREEAREDPEPLKNAPHTTPVRRLDEVYADRNLVLTWR 465
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
53-444 |
5.49e-150 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 433.58 E-value: 5.49e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 53 ELDLVRHYTELSNKNFGVDNGFYPLGSCTMKYNPKINEKVARIPG-FSESHPLQDEDQVQGSLEIIYSLQEELKEITGMD 131
Cdd:cd00613 1 ETEVLRHLKRLASKNKALDQSMSFLGSGTYKHNPPAVIKRNILENeFYTAYTPYQPEISQGRLQALFELQTMLCELTGMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 132 --EVTLQPAAGAHGEWTALMIFKAYHenngegHRDEVIVPDSAHGTNPASASFA----GFKSVTVKSNERGEVDIDDLKR 205
Cdd:cd00613 81 vaNASLQDEATAAAEAAGLAAIRAYH------KRNKVLVPDSAHPTNPAVARTRgeplGIEVVEVPSDEGGTVDLEALKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 206 VVNENTAAIMLTNPNTLGIFEKNIMEIREIVHNAGGLLYYDGANLNAIMdKVRPGDMGFDAVHLNLHKTF---------- 275
Cdd:cd00613 155 EVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNLTG-LKPPGEYGADIVVGNLQKTGvphggggpga 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 276 ----TgphggggpgsgpvgvVKELASYLPKPMVIKDGDKF----------KYDNDIKNSIGRVKPFYGNFGIYLRAYTYI 341
Cdd:cd00613 234 gffaV---------------KKELVRFLPGRLVGVTKDAEgnrafrlalqTREQHIRREKATSNICTGQALLALMAAMYI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 342 RTMGATGLKEVSEAAVLNANYIKARLSEHFEI-PYKQYCKHEFVLSGvrQKEFGVRTLDMAKRLLDFGVHPPTIYFPlnV 420
Cdd:cd00613 299 VYLGPEGLKEIAERAHLNANYLAKRLKEVGGVlPFNGPFFHEFVLRL--PPLYGIRAEDLAKALIDGGFHAPTMYLP--V 374
|
410 420
....*....|....*....|....
gi 581145584 421 EEGMMIEPTETESKETLDYFIDTL 444
Cdd:cd00613 375 DGTLMIEPTETETKEELDALLEAL 398
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
161-248 |
4.86e-05 |
|
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: 45.32 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 161 GHRDEVIVPDSAHGTN--PAS--ASFAGFKSVTVKSNERGEVDIDDLKRVVNENTA--AIMLTNpNTLGIFEkNIMEIRE 234
Cdd:pfam00266 86 KPGDEIVITEMEHHANlvPWQelAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKlvAITHVS-NVTGTIQ-PVPEIGK 163
|
90
....*....|....
gi 581145584 235 IVHNAGGLLYYDGA 248
Cdd:pfam00266 164 LAHQYGALVLVDAA 177
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
7-483 |
0e+00 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 908.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 7 PLIFERSREGRYAYSLPKSDIKTnSVESLLDDKFIRKNKAEFPEVAELDLVRHYTELSNKNFGVDNGFYPLGSCTMKYNP 86
Cdd:PRK04366 6 PLIFELSRPGRRGYSLPELDVPE-VLESLLPEELLRKEPPELPEVSELEVVRHYTRLSQKNYGVDTGFYPLGSCTMKYNP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 87 KINEKVARIPGFSESHPLQDEDQVQGSLEIIYSLQEELKEITGMDEVTLQPAAGAHGEWTALMIFKAYHENNGEGHRDEV 166
Cdd:PRK04366 85 KINEKVARLPGFAELHPLQPEETVQGALELMYELQEWLKEITGMDAVTLQPAAGAHGELTGLLMIRAYHEARGDTKRTEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 167 IVPDSAHGTNPASASFAGFKSVTVKSNERGEVDIDDLKRVVNENTAAIMLTNPNTLGIFEKNIMEIREIVHNAGGLLYYD 246
Cdd:PRK04366 165 IVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKAAVGEDTAALMLTNPNTLGLFERNILEIAEIVHEAGGLLYYD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 247 GANLNAIMDKVRPGDMGFDAVHLNLHKTFTgphggggpgsgpvgvvKELASYLPKPMVIKDGDKFKYDNDIKNSIGRVKP 326
Cdd:PRK04366 245 GANLNAILGKARPGDMGFDVVHLNLHKTFStphggggpgsgpvgvkEELAPFLPVPVVEKDGDRYRLDYDRPKSIGRVRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 327 FYGNFGIYLRAYTYIRTMGATGLKEVSEAAVLNANYIKARLSEHFEIPYKQYCKHEFVLSGVRQKEFGVRTLDMAKRLLD 406
Cdd:PRK04366 325 FYGNFGVLVRAYAYIRSLGAEGLREVSEDAVLNANYLKARLKDIYDLPYDRPCMHEFVLSGKKLKETGVRTLDIAKRLLD 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581145584 407 FGVHPPTIYFPLNVEEGMMIEPTETESKETLDYFIDTLISIAEEAKNDPDKVLEAPHTTVIDRLDEATAARKPILKF 483
Cdd:PRK04366 405 YGFHPPTIYFPLIVPEALMIEPTETESKETLDAFIAAMKQIAEEAKENPELVKEAPHNTPVRRLDEVKAARKPVLRW 481
|
|
| GcvP2 |
COG1003 |
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ... |
20-484 |
0e+00 |
|
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440627 Cd Length: 468 Bit Score: 808.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 20 YSLPKSDIktnSVESLLDDKFIRKNKAEFPEVAELDLVRHYTELSNKNFGVDNGFYPLGSCTMKYNPKINEKVARIPGFS 99
Cdd:COG1003 1 VSLPEPEA---DAASLLPEALLRKSPVFLPEVSETEVLRHYTRLSQKNLGLDTGMIPLGSCTMKYNPKINEEPATLPGFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 100 ESHPLQDEDQVQGSLEIIYSLQEELKEITGMDEVTLQPAAGAHGEWTALMIFKAYHENNGEGHRDEVIVPDSAHGTNPAS 179
Cdd:COG1003 78 NLHPFQPEETVQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGEGHRNEILIPDSAHGTNPAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 180 ASFAGFKSVTVKSNERGEVDIDDLKRVVNENTAAIMLTNPNTLGIFEKNIMEIREIVHNAGGLLYYDGANLNAIMDKVRP 259
Cdd:COG1003 158 AAMAGFKVVVVKSDEDGNVDLEDLKAKVGDRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 260 GDMGFDAVHLNLHKTFTgphggggpgsgpvgvvKELASYLPKPMVIKDGDKFKYDNDIKNSIGRVKPFYGNFGIYLRAYT 339
Cdd:COG1003 238 GDMGFDVCHLNLHKTFStphggggpgsgpvgvkEHLAPFLPGPPVVKDGDKYRLDYDRPKSIGRSAAFYGNAGVLVRAYA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 340 YIRTMGATGLKEVSEAAVLNANYIKARLSEHFEIPYK--QYCKHEFVLSGVRQK-EFGVRTLDMAKRLLDFGVHPPTIYF 416
Cdd:COG1003 318 YIRMMGAEGLREATEVAVLNANYLAARLKDHYPVLYTgnGRCAHEFILDLRPLKkETGVTTLDIAKRLLDYGFHAPTMYF 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581145584 417 PLNVEEGMMIEPTETESKETLDYFIDTLISIAEEAKNDPDKVLEAPHTTVIDRLDEATAARKPILKFE 484
Cdd:COG1003 398 PLIVPETLMIEPTESESKEELDRFIDAMIAIREEAREDPEPLKNAPHTTPVRRLDEVYADRNLVLTWR 465
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
53-444 |
5.49e-150 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 433.58 E-value: 5.49e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 53 ELDLVRHYTELSNKNFGVDNGFYPLGSCTMKYNPKINEKVARIPG-FSESHPLQDEDQVQGSLEIIYSLQEELKEITGMD 131
Cdd:cd00613 1 ETEVLRHLKRLASKNKALDQSMSFLGSGTYKHNPPAVIKRNILENeFYTAYTPYQPEISQGRLQALFELQTMLCELTGMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 132 --EVTLQPAAGAHGEWTALMIFKAYHenngegHRDEVIVPDSAHGTNPASASFA----GFKSVTVKSNERGEVDIDDLKR 205
Cdd:cd00613 81 vaNASLQDEATAAAEAAGLAAIRAYH------KRNKVLVPDSAHPTNPAVARTRgeplGIEVVEVPSDEGGTVDLEALKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 206 VVNENTAAIMLTNPNTLGIFEKNIMEIREIVHNAGGLLYYDGANLNAIMdKVRPGDMGFDAVHLNLHKTF---------- 275
Cdd:cd00613 155 EVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNLTG-LKPPGEYGADIVVGNLQKTGvphggggpga 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 276 ----TgphggggpgsgpvgvVKELASYLPKPMVIKDGDKF----------KYDNDIKNSIGRVKPFYGNFGIYLRAYTYI 341
Cdd:cd00613 234 gffaV---------------KKELVRFLPGRLVGVTKDAEgnrafrlalqTREQHIRREKATSNICTGQALLALMAAMYI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 342 RTMGATGLKEVSEAAVLNANYIKARLSEHFEI-PYKQYCKHEFVLSGvrQKEFGVRTLDMAKRLLDFGVHPPTIYFPlnV 420
Cdd:cd00613 299 VYLGPEGLKEIAERAHLNANYLAKRLKEVGGVlPFNGPFFHEFVLRL--PPLYGIRAEDLAKALIDGGFHAPTMYLP--V 374
|
410 420
....*....|....*....|....
gi 581145584 421 EEGMMIEPTETESKETLDYFIDTL 444
Cdd:cd00613 375 DGTLMIEPTETETKEELDALLEAL 398
|
|
| PLN02414 |
PLN02414 |
glycine dehydrogenase (decarboxylating) |
53-464 |
5.56e-111 |
|
glycine dehydrogenase (decarboxylating)
Pssm-ID: 178035 [Multi-domain] Cd Length: 993 Bit Score: 351.37 E-value: 5.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 53 ELDLVRHYTELSNKNFGVDNGFYPLGSCTMKYNPKINEKVARIPGFSESHPLQDEDQVQGSLEIIYSLQEELKEITGMDE 132
Cdd:PLN02414 506 EHELLRYLHRLQNKDLSLVHSMIPLGSCTMKLNATTEMMPVTWPEFANIHPFAPVDQAQGYQEMFEDLGDLLCEITGFDS 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 133 VTLQPAAGAHGEWTALMIFKAYHENNGEGHRDEVIVPDSAHGTNPASASFAGFKSVTVKSNERGEVDIDDLKRVV---NE 209
Cdd:PLN02414 586 FSLQPNAGAAGEYAGLMVIRAYHLSRGDHHRNVCIIPVSAHGTNPASAAMCGMKIVVVGTDAKGNINIEELRKAAeahKD 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 210 NTAAIMLTNPNTLGIFEKNIMEIREIVHNAGGLLYYDGANLNAIMDKVRPGDMGFDAVHLNLHKTFTGPHGGGGPGSGPV 289
Cdd:PLN02414 666 NLAALMVTYPSTHGVYEEGIDEICDIIHDNGGQVYMDGANMNAQVGLTSPGFIGADVCHLNLHKTFCIPHGGGGPGMGPI 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 290 GVVKELASYLPKPMVIKDGDKFKYDNdiknsigrVKPF-------YGNFGIYLRAYTYIRTMGATGLKEVSEAAVLNANY 362
Cdd:PLN02414 746 GVKKHLAPFLPSHPVVPTGGIPRPEK--------TQPLgtisaapWGSALILPISYTYIAMMGSEGLTDASKIAILNANY 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 363 IKARLSEHFEIPYK---QYCKHEFV--LSGVRQKEfGVRTLDMAKRLLDFGVHPPTIYFPlnVEEGMMIEPTETESKETL 437
Cdd:PLN02414 818 MAKRLEGHYPVLFRgknGTCAHEFIidLRPFKNTA-GIEPEDVAKRLMDYGFHAPTMSWP--VPGTLMIEPTESESKAEL 894
|
410 420 430
....*....|....*....|....*....|....*
gi 581145584 438 DYFIDTLISIAEE------AKNDP-DKVLE-APHT 464
Cdd:PLN02414 895 DRFCDALISIREEiadienGKADReNNVLKgAPHP 929
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
117-276 |
2.45e-17 |
|
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: 79.35 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 117 IYSLQEELKEIT--GMDEVTLQPAaGAHGEWTALMIFKAYHenngeghrDEVIVPDSAHGTNPASA---SFAGFKSVTVK 191
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVPS-GTGANEAALLALLGPG--------DEVIVDANGHGSRYWVAaelAGAKPVPVPVD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 192 SNERGEVDIDDLKRVVN-ENTAAIMLTNPNTLGIFEKNIMEIREIVHNAGGLLYYDGANLNAIMD--KVRPGDMGFDAVH 268
Cdd:cd01494 73 DAGYGGLDVAILEELKAkPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapGVLIPEGGADVVT 152
|
....*...
gi 581145584 269 LNLHKTFT 276
Cdd:cd01494 153 FSLHKNLG 160
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
30-444 |
2.93e-15 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 77.87 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 30 NSVESLLDD---KFIRKNKAEFPE-VAELDLVRHYTELSNKNFGVDN-------GFYPlgsctmKYNPKINEKVARIPGF 98
Cdd:PRK00451 22 KSIDELFADipeELRLKRPLDLPPgLSEMELLRHLRELAAKNKTAEEypsflgaGAYD------HYIPAVVDHIISRSEF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 99 SESH-PLQDEdqV-QGSLEIIYSLQEELKEITGMDEVTlqpaA----GAHGEWTALMIfkAYHENNgeghRDEVIVPDSA 172
Cdd:PRK00451 96 YTAYtPYQPE--IsQGTLQAIFEYQTMICELTGMDVAN----AsmydGATALAEAALM--AVRITK----RKKVLVSGAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 173 HgtnPAS-------ASFAGFKSVTVKSNErGEVDIDDLKRVVNENTAAIMLTNPNTLGIFEKnIMEIREIVHNAGGLLYy 245
Cdd:PRK00451 164 H---PEYrevlktyLKGQGIEVVEVPYED-GVTDLEALEAAVDDDTAAVVVQYPNFFGVIED-LEEIAEIAHAGGALFI- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 246 dgANLNAIMDKV--RPGDMGFDAV---------HLNL---HKTFtgphggggpgsgpvgvvkelasylpkpMVIKDgdkf 311
Cdd:PRK00451 238 --VGVDPVSLGLlkPPGEYGADIVvgegqplgiPLSFggpYLGF---------------------------FATRK---- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 312 KYdndIKNSIGRVkpfygnFGIYL-----RAYT--------YIR------------------------TMGATGLKEVSE 354
Cdd:PRK00451 285 KL---VRQMPGRL------VGETVdadgkRGFVltlqareqHIRrekatsnictnqalnalaaaiymsLLGPEGLRELAE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 355 AAVLNANYIKARLSEH-FEIPYKQYCKHEFVLsgvrqkEFGVRTLDMAKRLLDFGVH---PPTIYFPlNVEEGMMIEPTE 430
Cdd:PRK00451 356 QNHQKAHYLAERLAEIgGVELFDGPFFNEFVV------RLPKPAEEVNEALLEKGILggyDLGRYYP-ELGNHLLVCVTE 428
|
490
....*....|....
gi 581145584 431 TESKETLDYFIDTL 444
Cdd:PRK00451 429 KRTKEDIDALVAAL 442
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
111-444 |
1.13e-10 |
|
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: 63.51 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 111 QGSLEIIYSLQEELKEITGM--------DEVTlqpAAG-AhgewtALMIFKAyhenNGEGHRdeVIVPDSAHgtnPAS-- 179
Cdd:COG0403 108 QGRLQALFEFQTMVAELTGMdvanaslyDGAT---AAAeA-----MLMARRV----TKRSNK--VLVSEDVH---PQTra 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 180 -----ASFAGFKSVTVkSNERGEVDIDDLKRVVNENTAAIMLTNPNTLGIFEkNIMEIREIVHNAGGLLYYdGANLNA-- 252
Cdd:COG0403 171 vlktyAEPLGIEVVEV-PDEDGVTDLEALKALLDDDVAGVLVQYPNFFGVIE-DLRAIAEAAHAAGALVIV-AADPLSlg 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 253 IMdkVRPGDMGFDAV---------HLNL---HktftgphggggpgsgpvgvvkelASYlpkpMVIKDGDKFKYDNDIkns 320
Cdd:COG0403 248 LL--KPPGELGADIVvgegqrlgvPLGFggpH-----------------------AGF----FATREKLVRQMPGRL--- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 321 IGRVKPFYGNfgiylRAYT--------YIR------------------------TMGATGLKEVSEAAVLNANYIKARLS 368
Cdd:COG0403 296 VGVTVDADGK-----RAFRltlqtreqHIRrekatsnictnqallalaasmyavYHGPEGLKEIAERIHQKAHYLAERLA 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581145584 369 E-HFEIPYKQYCKHEFVLsgvrqkEFGVRTLDMAKRLLDFGVHPPtiyFPLNVEEG--MMIEPTETESKETLDYFIDTL 444
Cdd:COG0403 371 AlGVEVPFNGPFFDEFVV------RLPKPAAEINAALLEKGILGG---LNLRRVDDdtLLVAVTETTTKEDIDALVEAL 440
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
164-267 |
7.88e-06 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 47.75 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 164 DEVIVPDSAH------GtnpASASFAGFKSVTVKSnERGEVDIDDLKRVVNEN------TAAIMLTNPNTLG-IFEK-NI 229
Cdd:COG2008 75 DEVICHETAHiyvdegG---APEALSGVKLLPVPG-EDGKLTPEDLEAAIRPGdvhfpqPGLVSLENTTEGGtVYPLeEL 150
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 581145584 230 MEIREIVHNAGGLLYYDGANL-NAIM-DKVRPGDM--GFDAV 267
Cdd:COG2008 151 RAIAAVAREHGLPLHLDGARLfNAAAaLGVSLAEItaGVDSV 192
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
164-220 |
1.55e-05 |
|
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: 47.05 E-value: 1.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 581145584 164 DEVIVPDSAHGTNPASASFAGFKSVTVKSNERGE--VDIDDLKRVVNENTAAIMLTNPN 220
Cdd:COG0436 115 DEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENGflPDPEALEAAITPRTKAIVLNSPN 173
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
151-237 |
2.93e-05 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 46.04 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 151 FKAYHENNGEGHRD----EVIVPDSAHGTNPASASFAGFKSVTVKSNERGEVDIDDLKRVVNE------NTAAIMLTNPN 220
Cdd:cd06450 79 DRARKRLKAGGGRGidklVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGT 158
|
90
....*....|....*...
gi 581145584 221 T-LGIFEkNIMEIREIVH 237
Cdd:cd06450 159 TdTGAID-PLEEIADLAE 175
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
161-248 |
4.86e-05 |
|
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: 45.32 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 161 GHRDEVIVPDSAHGTN--PAS--ASFAGFKSVTVKSNERGEVDIDDLKRVVNENTA--AIMLTNpNTLGIFEkNIMEIRE 234
Cdd:pfam00266 86 KPGDEIVITEMEHHANlvPWQelAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKlvAITHVS-NVTGTIQ-PVPEIGK 163
|
90
....*....|....
gi 581145584 235 IVHNAGGLLYYDGA 248
Cdd:pfam00266 164 LAHQYGALVLVDAA 177
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
164-248 |
7.67e-05 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 44.74 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 164 DEVIVPDSAHGTN--P--ASASFAGFKSVTVKSNERGEVDIDDLKRVVNENTAAIMLTN-PNTLGIfeKN-IMEIREIVH 237
Cdd:COG0520 104 DEILITEMEHHSNivPwqELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHvSNVTGT--VNpVKEIAALAH 181
|
90
....*....|.
gi 581145584 238 NAGGLLYYDGA 248
Cdd:COG0520 182 AHGALVLVDGA 192
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
164-248 |
1.16e-04 |
|
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: 44.25 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 164 DEVIVPDSAHGTNPASASFAGFKSVTVKSNERG--EVDIDDLKRVVNENTAAIMLTNP-NTLGIF--EKNIMEIREIVHN 238
Cdd:cd00609 84 DEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGgfLLDLELLEAAKTPKTKLLYLNNPnNPTGAVlsEEELEELAELAKK 163
|
90
....*....|
gi 581145584 239 AGGLLYYDGA 248
Cdd:cd00609 164 HGILIISDEA 173
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
164-240 |
2.19e-04 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 43.64 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 164 DEVIVPDSAHGTNPASASFAGFKSVTVKS-NERG-EVDIDDLKRVVNENTAAIMLTNPN--TLGIFEKNimEIREIVHNA 239
Cdd:PRK08363 118 DEILIPGPSYPPYTGLVKFYGGVPVEYRTiEEEGwQPDIDDIRKKITEKTKAIAVINPNnpTGALYEKK--TLKEILDIA 195
|
.
gi 581145584 240 G 240
Cdd:PRK08363 196 G 196
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
164-220 |
2.67e-04 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 43.19 E-value: 2.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 581145584 164 DEVIVPDSAHGTNPASASFAGFKSVTVKSNE--RGEVDIDDLKRVVNENTAAIMLTNPN 220
Cdd:PRK05764 116 DEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEenGFKLTVEQLEAAITPKTKALILNSPS 174
|
|
| PRK13355 |
PRK13355 |
bifunctional HTH-domain containing protein/aminotransferase; Provisional |
164-236 |
1.40e-03 |
|
bifunctional HTH-domain containing protein/aminotransferase; Provisional
Pssm-ID: 237361 [Multi-domain] Cd Length: 517 Bit Score: 41.26 E-value: 1.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581145584 164 DEVIVPDSAHGTNPASASFAGFKSVTVKSNERGE--VDIDDLKRVVNENTAAIMLTNPN--TLGIFEKNIMEirEIV 236
Cdd:PRK13355 233 DEVLIPSPDYPLWTACVNLAGGTAVHYRCDEQSEwyPDIDDIRSKITSRTKAIVIINPNnpTGALYPREVLQ--QIV 307
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
132-271 |
1.79e-03 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 40.37 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 132 EVTLQPAAGAHGEWTALMIFKAYHEnngeghrDEVIVPDSAHGTNPASASFAGFKSVTVK--SNERGEVDIDDLKRVVNE 209
Cdd:pfam00155 63 EAAVVFGSGAGANIEALIFLLANPG-------DAILVPAPTYASYIRIARLAGGEVVRYPlyDSNDFHLDFDALEAALKE 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581145584 210 NTAAIMLTNP-NTLGIF--EKNIMEIREIVHNAGGLL-----YYDGAnlnaimdkvrPGDMGFDAVHLNL 271
Cdd:pfam00155 136 KPKVVLHTSPhNPTGTVatLEELEKLLDLAKEHNILLlvdeaYAGFV----------FGSPDAVATRALL 195
|
|
| |
