|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
12-418 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 763.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 12 DSVIAGAIAREMGRQRSEIELIASENIVSPAVLAAQGSVMTNKYAEGYPGHRYYGGCQYVDLVEAAAIERAGMLFDASFV 91
Cdd:PRK00011 10 DPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELFGAEYA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 92 NVQPHSGAQANGAVMLALLKPGDTFMGLSLAAGGHLTHGARPTMSGKWFNAVQYGVRESDCLIDYDELEVKAIATRPKLI 171
Cdd:PRK00011 90 NVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLALEHKPKLI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 172 ITGGSAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNPVEIADIVTTTTHKTLRGPRGGMILTNNQDVAKKV 251
Cdd:PRK00011 170 IAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTNDEELAKKI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 252 NSAVFPGLQGGPLMHVIAAKAVALGEALEDNFRQYARQMVANARALASALTERGYDIVSGGTDTHLILVDLRSKGVSGKD 331
Cdd:PRK00011 250 NSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 332 AEEALGRAGLTCNKNGIPFDPAPPAVTSGIRLGTPAATSRGFREAEFNEVGALIANVLDALGTEqsgEQERRARMSVHDL 411
Cdd:PRK00011 330 AEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDE---AVIEEVKEEVKEL 406
|
....*..
gi 1550121282 412 CAAFPIY 418
Cdd:PRK00011 407 CKRFPLY 413
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
12-418 |
0e+00 |
|
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439882 Cd Length: 414 Bit Score: 751.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 12 DSVIAGAIAREMGRQRSEIELIASENIVSPAVLAAQGSVMTNKYAEGYPGHRYYGGCQYVDLVEAAAIERAGMLFDASFV 91
Cdd:COG0112 9 DPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELFGAEHA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 92 NVQPHSGAQANGAVMLALLKPGDTFMGLSLAAGGHLTHGARPTMSGKWFNAVQYGVRESDCLIDYDELEVKAIATRPKLI 171
Cdd:COG0112 89 NVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLALEHKPKLI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 172 ITGGSAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNPVEIADIVTTTTHKTLRGPRGGMILTnNQDVAKKV 251
Cdd:COG0112 169 IAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILC-NEELAKKI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 252 NSAVFPGLQGGPLMHVIAAKAVALGEALEDNFRQYARQMVANARALASALTERGYDIVSGGTDTHLILVDLRSKGVSGKD 331
Cdd:COG0112 248 DSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 332 AEEALGRAGLTCNKNGIPFDPAPPAVTSGIRLGTPAATSRGFREAEFNEVGALIANVLDALGTEqsgEQERRARMSVHDL 411
Cdd:COG0112 328 AEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDE---AVLAEVREEVKEL 404
|
....*..
gi 1550121282 412 CAAFPIY 418
Cdd:COG0112 405 CKRFPLY 411
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
1-418 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 724.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 1 MPGLFERQLKH-DSVIAGAIAREMGRQRSEIELIASENIVSPAVLAAQGSVMTNKYAEGYPGHRYYGGCQYVDLVEAAAI 79
Cdd:PRK13034 1 LMFFFSDSLEEyDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 80 ERAGMLFDASFVNVQPHSGAQANGAVMLALLKPGDTFMGLSLAAGGHLTHGARPTMSGKWFNAVQYGVRESDCLIDYDEL 159
Cdd:PRK13034 81 ERAKQLFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 160 EVKAIATRPKLIITGGSAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNPVEIADIVTTTTHKTLRGPRGGM 239
Cdd:PRK13034 161 EELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 240 ILTNNQDVAKKVNSAVFPGLQGGPLMHVIAAKAVALGEALEDNFRQYARQMVANARALASALTERGYDIVSGGTDTHLIL 319
Cdd:PRK13034 241 ILTNDEEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 320 VDLRSKGVSGKDAEEALGRAGLTCNKNGIPFDPAPPAVTSGIRLGTPAATSRGFREAEFNEVGALIANVLDALGTEqsgE 399
Cdd:PRK13034 321 VDLRPKGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNA---A 397
|
410
....*....|....*....
gi 1550121282 400 QERRARMSVHDLCAAFPIY 418
Cdd:PRK13034 398 LEQRVRKEVKALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
12-389 |
0e+00 |
|
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.
Pssm-ID: 99733 Cd Length: 402 Bit Score: 603.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 12 DSVIAGAIAREMGRQRSEIELIASENIVSPAVLAAQGSVMTNKYAEGYPGHRYYGGCQYVDLVEAAAIERAGMLFDASFV 91
Cdd:cd00378 4 DPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 92 NVQPHSGAQANGAVMLALLKPGDTFMGLSLAAGGHLTHGARPT--MSGKWFNAVQYGVRESDCLIDYDELEVKAIATRPK 169
Cdd:cd00378 84 NVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFTKvsASGKLFESVPYGVDPETGLIDYDALEKMALEFKPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 170 LIITGGSAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNPVEIADIVTTTTHKTLRGPRGGMILTNNQDVAK 249
Cdd:cd00378 164 LIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKGELAK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 250 KVNSAVFPGLQGGPLMHVIAAKAVALGEALEDNFRQYARQMVANARALASALTERGYDIVSGGTDTHLILVDLRSKGVSG 329
Cdd:cd00378 244 KINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGITG 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 330 KDAEEALGRAGLTCNKNGIPFDPAPPAVTSGIRLGTPAATSRGFREAEFNEVGALIANVL 389
Cdd:cd00378 324 KAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARAL 383
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
12-385 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 592.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 12 DSVIAGAIAREMGRQRSEIELIASENIVSPAVLAAQGSVMTNKYAEGYPGHRYYGGCQYVDLVEAAAIERAGMLFDAS-- 89
Cdd:pfam00464 5 DPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDpa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 90 --FVNVQPHSGAQANGAVMLALLKPGDTFMGLSLAAGGHLTHGA-----RPTMSGKWFNAVQYGVRESDCLIDYDELEVK 162
Cdd:pfam00464 85 kwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYpvnskKISASSKFFESMPYGVDPETGYIDYDQLEKN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 163 AIATRPKLIITGGSAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNPVEIADIVTTTTHKTLRGPRGGMILT 242
Cdd:pfam00464 165 AKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIFY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 243 NN-------------QDVAKKVNSAVFPGLQGGPLMHVIAAKAVALGEALEDNFRQYARQMVANARALASALTERGYDIV 309
Cdd:pfam00464 245 RKgvksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYKLV 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121282 310 SGGTDTHLILVDLRSKGVSGKDAEEALGRAGLTCNKNGIPFDPApPAVTSGIRLGTPAATSRGFREAEFNEVGALI 385
Cdd:pfam00464 325 SGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKS-AFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
10-390 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 516.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 10 KHDSVIAGAIAREMGRQRSEIELIASENIVSPAVLAAQGSVMTNKYAEGYPGHRYYGGCQYVDLVEAAAIERAGMLFDAS 89
Cdd:PTZ00094 17 EADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFGLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 90 F----VNVQPHSGAQANGAVMLALLKPGDTFMGLSLAAGGHLTHG-----ARPTMSGKWFNAVQYGVREsDCLIDYDELE 160
Cdd:PTZ00094 97 PeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNE-KGLIDYDKLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 161 VKAIATRPKLIITGGSAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNPVEIADIVTTTTHKTLRGPRGGMI 240
Cdd:PTZ00094 176 ELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSGLI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 241 LTN---NQDVAKKVNSAVFPGLQGGPLMHVIAAKAVALGEALEDNFRQYARQMVANARALASALTERGYDIVSGGTDTHL 317
Cdd:PTZ00094 256 FYRkkvKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDNHL 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121282 318 ILVDLRSKGVSGKDAEEALGRAGLTCNKNGIPFD---PAPpavtSGIRLGTPAATSRGFREAEFnevgALIANVLD 390
Cdd:PTZ00094 336 VLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDksaLNP----SGVRLGTPALTTRGAKEKDF----KFVADFLD 403
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
15-418 |
6.21e-168 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 480.31 E-value: 6.21e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 15 IAGAIAREMGRQRSEIELIASENIVSPAVLAAQGSVMTNKYAEGYPGHRYYGGCQYVDLVEAAAIERAGMLFDASFVNVQ 94
Cdd:PRK13580 37 IAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAYVQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 95 PHSGAQAN--------------------GAVMLALLKPGDTF-----------MGLSLAAGGHLTHGARPTMSGKWFNAV 143
Cdd:PRK13580 117 PHSGADANlvafwailahkvespaleklGAKTVNDLTEEDWEalraelgnqrlLGMSLDSGGHLTHGFRPNISGKMFHQR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 144 QYGVRESDCLIDYDELEVKAIATRPKLIITGGSAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGV---HPNPVEI 220
Cdd:PRK13580 197 SYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVftgDEDPVPH 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 221 ADIVTTTTHKTLRGPRGGMILTNnQDVAKKVNSAVfPGLQGGPLMHVIAAKAVALGEALEDNFRQYARQMVANARALASA 300
Cdd:PRK13580 277 ADIVTTTTHKTLRGPRGGLVLAK-KEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAEG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 301 LTERGYDIVSGGTDTHLILVDLRSKGVSGKDAEEALGRAGLTCNKNGIPFDPAPPAVTSGIRLGTPAATSRGFREAEFNE 380
Cdd:PRK13580 355 FLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLGMGSDEMDE 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1550121282 381 VGALIANVLDA--LGTEQSGEQER-----------RARMSVHDLCAAFPIY 418
Cdd:PRK13580 435 VAELIVKVLSNttPGTTAEGAPSKakyeldegvaqEVRARVAELLARFPLY 485
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
11-385 |
3.68e-163 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 467.54 E-value: 3.68e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 11 HDSVIAGAIAREMGRQRSEIELIASENIVSPAVLAAQGSVMTNKYAEGYPGHRYYGGCQYVDLVEAAAIERAGMLFDASF 90
Cdd:PLN03226 18 VDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFRLDP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 91 ----VNVQPHSGAQANGAVMLALLKPGDTFMGLSLAAGGHLTHGARpTMSGK------WFNAVQYGVRESDCLIDYDELE 160
Cdd:PLN03226 98 ekwgVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQ-TDGKKisatsiYFESMPYRLDESTGLIDYDKLE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 161 VKAIATRPKLIITGGSAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNPVEIADIVTTTTHKTLRGPRGGMI 240
Cdd:PLN03226 177 KKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGGMI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 241 -------LTNNQ------DVAKKVNSAVFPGLQGGPLMHVIAAKAVALGEALEDNFRQYARQMVANARALASALTERGYD 307
Cdd:PLN03226 257 ffrkgpkPPKGQgegavyDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKGYK 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121282 308 IVSGGTDTHLILVDLRSKGVSGKDAEEALGRAGLTCNKNGIPFDpAPPAVTSGIRLGTPAATSRGFREAEFNEVGALI 385
Cdd:PLN03226 337 LVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVEKDFEKVAEFL 413
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
12-389 |
1.98e-113 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 344.10 E-value: 1.98e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 12 DSVIAGAIAREMGRQRSEIELIASENIVSPAVLAAQGSVMTNKYAEGYPGHRYYGGCQYVDLVEAAAIERAGMLF----D 87
Cdd:PLN02271 133 DPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFgldsE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 88 ASFVNVQPHSGAQANGAVMLALLKPGDTFMGLSLAAGGHLTHGARpTMSGK-------WFNAVQYGVRESDCLIDYDELE 160
Cdd:PLN02271 213 KWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYY-TPGGKkvsgasiFFESLPYKVNPQTGYIDYDKLE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 161 VKAIATRPKLIITGGSAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNPVEIADIVTTTTHKTLRGPRGGMI 240
Cdd:PLN02271 292 EKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGII 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 241 L------------------TNNQ-DVAKKVNSAVFPGLQGGPLMHVIAAKAVALGEALEDNFRQYARQMVANARALASAL 301
Cdd:PLN02271 372 FyrkgpklrkqgmllshgdDNSHyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASAL 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 302 TERGYDIVSGGTDTHLILVDLRSKGVSGKDAEEALGRAGLTCNKNGIpFDPAPPAVTSGIRLGTPAATSRGFREAEFNEV 381
Cdd:PLN02271 452 LRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAI-FGDNGTISPGGVRIGTPAMTSRGCLESDFETI 530
|
410
....*....|....
gi 1550121282 382 ------GALIANVL 389
Cdd:PLN02271 531 adfllrAAQIASAV 544
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
75-243 |
1.22e-21 |
|
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: 91.29 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 75 EAAAIERAGMLFDASFVN-VQPHSGAQANGAVMLALLKPGDTFMGLSLAAGGHLTHGArpTMSGKWFNAVQYGvRESDCL 153
Cdd:cd01494 2 LEELEEKLARLLQPGNDKaVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVAA--ELAGAKPVPVPVD-DAGYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 154 IDYDELEVKAIATRPKLIITGGSAYPR--LIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNPVEIADIVTTTTHKT 231
Cdd:cd01494 79 LDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKN 158
|
170
....*....|..
gi 1550121282 232 LRGPRGGMILTN 243
Cdd:cd01494 159 LGGEGGGVVIVK 170
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
62-357 |
1.89e-12 |
|
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: 68.14 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 62 HRYYGGCQYVDLVEAAA---IERAGMLFDASFVnVQPHSGAQANGAVMLALLKPGD-------TFMGLSLAAgghLTHGA 131
Cdd:cd00609 30 LGYYPDPGLPELREAIAewlGRRGGVDVPPEEI-VVTNGAQEALSLLLRALLNPGDevlvpdpTYPGYEAAA---RLAGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 132 RPtmsgkwfnaVQYGVRESDCLIDYDELEVKAIATRPKLII-------TGgsAYPRLIDFKRIRAIADSVGAAMMVDMAH 204
Cdd:cd00609 106 EV---------VPVPLDEEGGFLLDLELLEAAKTPKTKLLYlnnpnnpTG--AVLSEEELEELAELAKKHGILIISDEAY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 205 fAGLVAGGVHPNPVEIAD-----IVTTTTHKTLRGP--RGGMILTNNQDVAKKVNSAVfPGLQGGPLMHVIAAKAVALGE 277
Cdd:cd00609 175 -AELVYDGEPPPALALLDayervIVLRSFSKTFGLPglRIGYLIAPPEELLERLKKLL-PYTTSGPSTLSQAAAAAALDD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 278 AlEDNFRQYARQMVANARALASALTERGYDIVSGGTDTHLILVDLrSKGVSGKDAEEALGRAGLTCNKNGIPFDPAPPAV 357
Cdd:cd00609 253 G-EEHLEELRERYRRRRDALLEALKELGPLVVVKPSGGFFLWLDL-PEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGFV 330
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
65-309 |
6.16e-08 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 54.23 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 65 YGGCQYVDLVEAAAIERAGMLFDASF---VNVQPHSGAQAN-GAVMLALLKPGDTFMGLSLAAGGHlTHGARpTMSGKWf 140
Cdd:pfam00155 35 YGPTDGHPELREALAKFLGRSPVLKLdreAAVVFGSGAGANiEALIFLLANPGDAILVPAPTYASY-IRIAR-LAGGEV- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 141 naVQYGVRES-DCLIDYDELEvKAIATRPKLIITG------GSAYPRLiDFKRIRAIADSVGAAMMVDMAHfAGLVAGGV 213
Cdd:pfam00155 112 --VRYPLYDSnDFHLDFDALE-AALKEKPKVVLHTsphnptGTVATLE-ELEKLLDLAKEHNILLLVDEAY-AGFVFGSP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 214 HPNPV------EIADIVTTTTHKT--LRGPRGGMILTNnQDVAKKVNSAVFPGLQGGPLmhVIAAKAVALGEALEDNF-R 284
Cdd:pfam00155 187 DAVATrallaeGPNLLVVGSFSKAfgLAGWRVGYILGN-AAVISQLRKLARPFYSSTHL--QAAAAAALSDPLLVASElE 263
|
250 260
....*....|....*....|....*
gi 1550121282 285 QYARQMVANARALASALTERGYDIV 309
Cdd:pfam00155 264 EMRQRIKERRDYLRDGLQAAGLSVL 288
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
40-323 |
2.52e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 42.59 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 40 SPAVLAAQGSVMTnkyaegypGHRYYGGCQYVDLVEAAAIERAGmlFDAS-FVnvqpHSGAQANGAVMLALLKPGDtfmG 118
Cdd:pfam01212 11 TPAMREAMAAAMV--------GDEVYGGDPTVNRLEDRVAELFG--KEAAlFV----PSGTAANQLALMAHCQRGD---E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 119 LSLAAGGHL---THGARPTMSGKWFNAVqygVRESDCLIDYDELE------VKAIATRPKLI-------ITGGSAYPrLI 182
Cdd:pfam01212 74 VICGEPAHIhfdETGGHAELGGVQPRPL---DGDEAGNMDLEDLEaairevGADIFPPTGLIslenthnSAGGQVVS-LE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 183 DFKRIRAIADSVGAAMMVDMAHFA-GLVAGGVHPNPV-EIADIVTTTTHKTLRGPRGGMILTNNQDVAKKVNsavFPGLQ 260
Cdd:pfam01212 150 NLREIAALAREHGIPVHLDGARFAnAAVALGVIVKEItSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIR---QRKYL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121282 261 GGPL--MHVIAAKAVAlgeALEDNFRQYARQmVANARALASALTERGYDIVSgGTDTHLILVDLR 323
Cdd:pfam01212 227 GGGLrqAGVLAAAGLR---ALEEGVARLARD-HATARRLAEGLELLRLAIPR-RVYTNTHMVYVA 286
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
95-251 |
3.73e-04 |
|
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: 42.27 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 95 PHSGAQANG--AVMLAL----LKPGD-------TFMGLSLAAgghLTHGARPtmsgkwfnaVQYGVRESDCLIDYDELEv 161
Cdd:pfam01041 40 KHAIAVSSGtaALHLALralgVGPGDevitpsfTFVATANAA---LRLGAKP---------VFVDIDPDTYNIDPEAIE- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 162 KAIATRPKLIItGGSAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNpvEIADIVTTTTH--KTLRGPRGGM 239
Cdd:pfam01041 107 AAITPRTKAII-PVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG--TLGDAATFSFHptKNLTTGEGGA 183
|
170
....*....|..
gi 1550121282 240 ILTNNQDVAKKV 251
Cdd:pfam01041 184 VVTNDPELAEKA 195
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
88-251 |
5.97e-04 |
|
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: 41.76 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 88 ASFVNVqPHSGAQANG--AVMLAL----LKPGD-------TFMGLSLAAgghLTHGARPTMSGkwfnavqygVRESDCLI 154
Cdd:cd00616 28 AEYLGV-KYAVAVSSGtaALHLALralgIGPGDevivpsfTFVATANAI---LLLGATPVFVD---------IDPDTYNI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 155 DYDELEvKAIATRPKLII----TGGSAyprliDFKRIRAIADSVGAAMMVDMAHFAGLVAGGVHPNpvEIADIVTTTTH- 229
Cdd:cd00616 95 DPELIE-AAITPRTKAIIpvhlYGNPA-----DMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVG--TFGDAGAFSFHp 166
|
170 180
....*....|....*....|...
gi 1550121282 230 -KTLRGPRGGMILTNNQDVAKKV 251
Cdd:cd00616 167 tKNLTTGEGGAVVTNDEELAERA 189
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
155-320 |
2.28e-03 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 39.79 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 155 DYDELEVKAIAT-----RPKLIITGG--SAYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLV----AGGV-HPNPVEIAD 222
Cdd:PRK06939 157 DMADLEAQLKEAkeagaRHKLIATDGvfSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVgengRGTVeHFGVMDRVD 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 223 IVTTTTHKTLRGPRGGMIlTNNQDVAK--KVNSAvfPGLQGGPLMHVIAAKAVALGEALEDNfRQYARQMVANARALASA 300
Cdd:PRK06939 237 IITGTLGKALGGASGGYT-AGRKEVIDwlRQRSR--PYLFSNSLAPAIVAASIKVLELLEES-DELRDRLWENARYFREG 312
|
170 180
....*....|....*....|
gi 1550121282 301 LTERGYDIvsGGTDTHLILV 320
Cdd:PRK06939 313 MTAAGFTL--GPGEHPIIPV 330
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
151-237 |
8.38e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 38.20 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121282 151 DCLIDYDELEvKAIATRPKLI-ITGGS-AYPRLIDFKRIRAIADSVGAAMMVDMAHFAGLVaggvhpnPVEI----ADIV 224
Cdd:COG0520 139 DGELDLEALE-ALLTPRTKLVaVTHVSnVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHL-------PVDVqalgCDFY 210
|
90
....*....|...
gi 1550121282 225 TTTTHKtLRGPRG 237
Cdd:COG0520 211 AFSGHK-LYGPTG 222
|
|
| |
