|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
1-412 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 842.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 1 MSYITKQDKVIAEAIEREFQRQNSNIELIASENFVSEAVMEAQGSVLTNKYAEGYPGRRYYGGCEFVDVTESIAIDRAKA 80
Cdd:PRK00011 3 MDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 81 LFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGAPVNFSGKFYNFVEYGVDKDTERINYDEVRKLAL 160
Cdd:PRK00011 83 LFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 161 EHKPKLIVAGASAYSRTIDFKKFKEIADEVNAKLMVDMAHIAGLVAAGLHPNPVEYADFVTTTTHKTLRGPRGGMILCK- 239
Cdd:PRK00011 163 EHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTNd 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 240 EEYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALENNFKMYQQQVVKNAKVLAETLINEGFRIVSGGTDNHLVAVDVKg 319
Cdd:PRK00011 243 EELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLR- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 320 SIGLTGKEAEETLDSVGITCNKNTIPFDQEKPFVTSGIRLGTPAATTRGFDEKAFEEVAKIISLALKNSKDEEKLQQAKE 399
Cdd:PRK00011 322 SKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKE 401
|
410
....*....|...
gi 612660568 400 RVAKLTAEYPLYQ 412
Cdd:PRK00011 402 EVKELCKRFPLYK 414
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
1-411 |
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: 836.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 1 MSYITKQDKVIAEAIEREFQRQNSNIELIASENFVSEAVMEAQGSVLTNKYAEGYPGRRYYGGCEFVDVTESIAIDRAKA 80
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 81 LFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGAPVNFSGKFYNFVEYGVDKDTERINYDEVRKLAL 160
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 161 EHKPKLIVAGASAYSRTIDFKKFKEIADEVNAKLMVDMAHIAGLVAAGLHPNPVEYADFVTTTTHKTLRGPRGGMILCKE 240
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 241 EYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALENNFKMYQQQVVKNAKVLAETLINEGFRIVSGGTDNHLVAVDVKgS 320
Cdd:COG0112 242 ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLR-S 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 321 IGLTGKEAEETLDSVGITCNKNTIPFDQEKPFVTSGIRLGTPAATTRGFDEKAFEEVAKIISLALKNSKDEEKLQQAKER 400
Cdd:COG0112 321 KGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREE 400
|
410
....*....|.
gi 612660568 401 VAKLTAEYPLY 411
Cdd:COG0112 401 VKELCKRFPLY 411
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
1-411 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 704.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 1 MSYITKQDKVIAEAIEREFQRQNSNIELIASENFVSEAVMEAQGSVLTNKYAEGYPGRRYYGGCEFVDVTESIAIDRAKA 80
Cdd:PRK13034 6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 81 LFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGAPVNFSGKFYNFVEYGVDKDTERINYDEVRKLAL 160
Cdd:PRK13034 86 LFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEELAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 161 EHKPKLIVAGASAYSRTIDFKKFKEIADEVNAKLMVDMAHIAGLVAAGLHPNPVEYADFVTTTTHKTLRGPRGGMILCK- 239
Cdd:PRK13034 166 EHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNd 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 240 EEYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALENNFKMYQQQVVKNAKVLAETLINEGFRIVSGGTDNHLVAVDVKG 319
Cdd:PRK13034 246 EEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 320 SiGLTGKEAEETLDSVGITCNKNTIPFDQEKPFVTSGIRLGTPAATTRGFDEKAFEEVAKIISLALKNSKDEEKLQQAKE 399
Cdd:PRK13034 326 K-GLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRK 404
|
410
....*....|..
gi 612660568 400 RVAKLTAEYPLY 411
Cdd:PRK13034 405 EVKALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
6-404 |
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: 663.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 6 KQDKVIAEAIEREFQRQNSNIELIASENFVSEAVMEAQGSVLTNKYAEGYPGRRYYGGCEFVDVTESIAIDRAKALFGAE 85
Cdd:cd00378 2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 86 HVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGAP--VNFSGKFYNFVEYGVDKDTERINYDEVRKLALEHK 163
Cdd:cd00378 82 YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 164 PKLIVAGASAYSRTIDFKKFKEIADEVNAKLMVDMAHIAGLVAAGLHPNPVEYADFVTTTTHKTLRGPRGGMILC-KEEY 242
Cdd:cd00378 162 PKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTrKGEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 243 KKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALENNFKMYQQQVVKNAKVLAETLINEGFRIVSGGTDNHLVAVDVKgSIG 322
Cdd:cd00378 242 AKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLR-PKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 323 LTGKEAEETLDSVGITCNKNTIPFDQEKPFVTSGIRLGTPAATTRGFDEKAFEEVAKIISLALKNSKDEEKLQQAKERVA 402
Cdd:cd00378 321 ITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVA 400
|
..
gi 612660568 403 KL 404
Cdd:cd00378 401 EL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
7-381 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 626.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 7 QDKVIAEAIEREFQRQNSNIELIASENFVSEAVMEAQGSVLTNKYAEGYPGRRYYGGCEFVDVTESIAIDRAKALFGAE- 85
Cdd:pfam00464 4 SDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 86 ---HVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGAPVNF-----SGKFYNFVEYGVDKDTERINYDEVRK 157
Cdd:pfam00464 84 akwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQLEK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 158 LALEHKPKLIVAGASAYSRTIDFKKFKEIADEVNAKLMVDMAHIAGLVAAGLHPNPVEYADFVTTTTHKTLRGPRGGMIL 237
Cdd:pfam00464 164 NAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 238 CK--------------EEYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALENNFKMYQQQVVKNAKVLAETLINEGFRI 303
Cdd:pfam00464 244 YRkgvksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYKL 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612660568 304 VSGGTDNHLVAVDVKgSIGLTGKEAEETLDSVGITCNKNTIPFDqEKPFVTSGIRLGTPAATTRGFDEKAFEEVAKII 381
Cdd:pfam00464 324 VSGGTDNHLVLVDLR-PKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
6-410 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 521.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 6 KQDKVIAEAIEREFQRQNSNIELIASENFVSEAVMEAQGSVLTNKYAEGYPGRRYYGGCEFVDVTESIAIDRAKALFGAE 85
Cdd:PTZ00094 17 EADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFGLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 86 H----VNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHG-----APVNFSGKFYNFVEYGVDKDTErINYDEVR 156
Cdd:PTZ00094 97 PeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEKGL-IDYDKLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 157 KLALEHKPKLIVAGASAYSRTIDFKKFKEIADEVNAKLMVDMAHIAGLVAAGLHPNPVEYADFVTTTTHKTLRGPRGGMI 236
Cdd:PTZ00094 176 ELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSGLI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 237 LCKEEYKKD----IDKTIFPGIQGGPLEHVIAAKAVAFGEALENNFKMYQQQVVKNAKVLAETLINEGFRIVSGGTDNHL 312
Cdd:PTZ00094 256 FYRKKVKPDienkINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDNHL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 313 VAVDVKgSIGLTGKEAEETLDSVGITCNKNTIPFDQEKpFVTSGIRLGTPAATTRGFDEKAFEEVAKIISLALKNSKD-- 390
Cdd:PTZ00094 336 VLVDLR-PFGITGSKMEKLLDAVNISVNKNTIPGDKSA-LNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVKLAQEiq 413
|
410 420 430
....*....|....*....|....*....|....*.
gi 612660568 391 ----------------EEKLQQAKERVAKLTAEYPL 410
Cdd:PTZ00094 414 kqvgkklvdfkkalekNPELQKLRQEVVEFASQFPF 449
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
11-411 |
0e+00 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 518.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 11 IAEAIEREFQRQNSNIELIASENFVSEAVMEAQGSVLTNKYAEGYPGRRYYGGCEFVDVTESIAIDRAKALFGAEHVNVQ 90
Cdd:PRK13580 37 IAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAYVQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 91 PHSGSQANMAVYLVAL------------------------------EMGDTV-LGMNLSHGGHLTHGAPVNFSGKFYNFV 139
Cdd:PRK13580 117 PHSGADANLVAFWAILahkvespaleklgaktvndlteedwealraELGNQRlLGMSLDSGGHLTHGFRPNISGKMFHQR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 140 EYGVDKDTERINYDEVRKLALEHKPKLIVAGASAYSRTIDFKKFKEIADEVNAKLMVDMAHIAGLVAAGL---HPNPVEY 216
Cdd:PRK13580 197 SYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVftgDEDPVPH 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 217 ADFVTTTTHKTLRGPRGGMILCKEEYKKDIDKTIfPGIQGGPLEHVIAAKAVAFGEALENNFKMYQQQVVKNAKVLAETL 296
Cdd:PRK13580 277 ADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAEGF 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 297 INEGFRIVSGGTDNHLVAVDVkGSIGLTGKEAEETLDSVGITCNKNTIPFDQEKPFVTSGIRLGTPAATTRGFDEKAFEE 376
Cdd:PRK13580 356 LKRGARLVTGGTDNHLVLIDV-TSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLGMGSDEMDE 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 612660568 377 VAKIISLALKNSK----------------DEEKLQQAKERVAKLTAEYPLY 411
Cdd:PRK13580 435 VAELIVKVLSNTTpgttaegapskakyelDEGVAQEVRARVAELLARFPLY 485
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
7-396 |
6.03e-166 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 474.08 E-value: 6.03e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 7 QDKVIAEAIEREFQRQNSNIELIASENFVSEAVMEAQGSVLTNKYAEGYPGRRYYGGCEFVDVTESIAIDRAKALFGAEH 86
Cdd:PLN03226 18 VDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFRLDP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 87 ----VNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHG-----APVNFSGKFYNFVEYGVDKDTERINYDEVRK 157
Cdd:PLN03226 98 ekwgVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtdgKKISATSIYFESMPYRLDESTGLIDYDKLEK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 158 LALEHKPKLIVAGASAYSRTIDFKKFKEIADEVNAKLMVDMAHIAGLVAAGLHPNPVEYADFVTTTTHKTLRGPRGGMIL 237
Cdd:PLN03226 178 KAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGGMIF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 238 CKE--------------EYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALENNFKMYQQQVVKNAKVLAETLINEGFRI 303
Cdd:PLN03226 258 FRKgpkppkgqgegavyDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKGYKL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 304 VSGGTDNHLVAVDVKgSIGLTGKEAEETLDSVGITCNKNTIPFDQEKpFVTSGIRLGTPAATTRGFDEKAFEEVA----K 379
Cdd:PLN03226 338 VTGGTDNHLVLWDLR-PLGLTGSRVEKVLDLAHITLNKNAVPGDSSA-LVPGGVRIGTPAMTSRGLVEKDFEKVAeflhR 415
|
410
....*....|....*..
gi 612660568 380 IISLALKNSKDEEKLQQ 396
Cdd:PLN03226 416 AVTIALKIQKEHGKKLK 432
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
4-378 |
6.48e-117 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 352.96 E-value: 6.48e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 4 ITKQDKVIAEAIEREFQRQNSNIELIASENFVSEAVMEAQGSVLTNKYAEGYPGRRYYGGCEFVDVTESIAIDRAKALFG 83
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 84 AEH----VNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHG------APVNFSGKFYNFVEYGVDKDTERINYD 153
Cdd:PLN02271 209 LDSekwgVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyytpggKKVSGASIFFESLPYKVNPQTGYIDYD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 154 EVRKLALEHKPKLIVAGASAYSRTIDFKKFKEIADEVNAKLMVDMAHIAGLVAAGLHPNPVEYADFVTTTTHKTLRGPRG 233
Cdd:PLN02271 289 KLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 234 GMILCKE--------------------EYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALENNFKMYQQQVVKNAKVLA 293
Cdd:PLN02271 369 GIIFYRKgpklrkqgmllshgddnshyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 294 ETLINEGFRIVSGGTDNHLVAVDVKgSIGLTGKEAEETLDSVGITCNKNTIpFDQEKPFVTSGIRLGTPAATTRGFDEKA 373
Cdd:PLN02271 449 SALLRRKCRLVTGGTDNHLLLWDLT-TLGLTGKNYEKVCEMCHITLNKTAI-FGDNGTISPGGVRIGTPAMTSRGCLESD 526
|
....*
gi 612660568 374 FEEVA 378
Cdd:PLN02271 527 FETIA 531
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
74-236 |
5.05e-26 |
|
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: 103.23 E-value: 5.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 74 AIDRAKALF--GAEHVNVQPhSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGAPVnfsgKFYNFVEYGVDKDTER-I 150
Cdd:cd01494 5 LEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAEL----AGAKPVPVPVDDAGYGgL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 151 NYDEVRKLALEHKPKLIVAGASAYSRTI--DFKKFKEIADEVNAKLMVDMAHIAGLVAAGLHPNPVEYADFVTTTTHKTL 228
Cdd:cd01494 80 DVAILEELKAKPNVALIVITPNTTSGGVlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNL 159
|
....*...
gi 612660568 229 RGPRGGMI 236
Cdd:cd01494 160 GGEGGGVV 167
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
74-242 |
1.26e-06 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 49.55 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 74 AIDRAKALFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGH-----LTHGAPVnfsgkfynFVEYGVDKDTE 148
Cdd:cd00615 64 AQELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVinglvLSGAVPV--------YLKPERNPYYG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 149 ---RINYDEVRKLALEHK-PKLIVAGASAYSRTI-DFKKFKEIADEVNAKLMVDMAHIAglvAAGLHPN-PVEY----AD 218
Cdd:cd00615 136 iagGIPPETFKKALIEHPdAKAAVITNPTYYGICyNLRKIVEEAHHRGLPVLVDEAHGA---HFRFHPIlPSSAamagAD 212
|
170 180
....*....|....*....|....*
gi 612660568 219 FVTTTTHKTLRGPR-GGMILCKEEY 242
Cdd:cd00615 213 IVVQSTHKTLPALTqGSMIHVKGDL 237
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
34-304 |
2.63e-06 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 48.84 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 34 FVSEAVMEAQGSVLTNKYAEGYPGRRYYggcefVDVTESIAidrakALFGAEHV-------NVQPHSGSQANMAVYLVAL 106
Cdd:pfam00155 14 DTLPAVAKAEKDALAGGTRNLYGPTDGH-----PELREALA-----KFLGRSPVlkldreaAVVFGSGAGANIEALIFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 107 EM-GDTVLGMNLSHGGHLT----HGAPVnfsgKFYNFVeygvDKDTERINYDEVRKlALEHKPKLIVAgASAYSRT---I 178
Cdd:pfam00155 84 ANpGDAILVPAPTYASYIRiarlAGGEV----VRYPLY----DSNDFHLDFDALEA-ALKEKPKVVLH-TSPHNPTgtvA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 179 DFKKFKEIADEVNAK---LMVDMAHIAG----LVAAGLHPNPVEYAD-FVTTTTHKT--LRGPRGGMILCKEEYKKDIDK 248
Cdd:pfam00155 154 TLEELEKLLDLAKEHnilLLVDEAYAGFvfgsPDAVATRALLAEGPNlLVVGSFSKAfgLAGWRVGYILGNAAVISQLRK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 612660568 249 TIFPGIQGGPLEHvIAAKAVAFGEALENNFKMYQQQVVKNAKVLAETLINEGFRIV 304
Cdd:pfam00155 234 LARPFYSSTHLQA-AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVL 288
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
151-305 |
4.76e-06 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 48.47 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 151 NYDEVRKLALEHKPKLIVAGaSAYSRTIDF---KKFKEIADEVNAKLMVDMAHI--------AGLVAA-GLhpnpVEYAD 218
Cdd:PRK07179 169 DVDHLRRQIERHGPGIIVVD-SVYSTTGTIaplADIVDIAEEFGCVLVVDESHSlgthgpqgAGLVAElGL----TSRVH 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 219 FVTTTTHKTLRGpRGGMILCKEEYKKDIDKTIFPGI-QGGPLEHVIA--AKAVAFGEALENNfkmyQQQVVKNAKVLAET 295
Cdd:PRK07179 244 FITASLAKAFAG-RAGIITCPRELAEYVPFVSYPAIfSSTLLPHEIAglEATLEVIESADDR----RARLHANARFLREG 318
|
170
....*....|
gi 612660568 296 LINEGFRIVS 305
Cdd:PRK07179 319 LSELGYNIRS 328
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
92-381 |
5.91e-06 |
|
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: 48.11 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 92 HSGSQANMAVYLVALEMGDTVLGMNLSHGGHLT----HGAPVnfsgkfynfVEYGVDKDTERINYDEVRKLALEHKPKLI 167
Cdd:cd00609 66 NGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAaarlAGAEV---------VPVPLDEEGGFLLDLELLEAAKTPKTKLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 168 V-------AGAsAYSRTiDFKKFKEIADEVNAKLMVDMAHiAGLVAAGLHPNPVEYAD-----FVTTTTHKTLRGP--RG 233
Cdd:cd00609 137 YlnnpnnpTGA-VLSEE-ELEELAELAKKHGILIISDEAY-AELVYDGEPPPALALLDayervIVLRSFSKTFGLPglRI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 234 GMILCKEEYKKDIDKTIFPGIQGGPleHVIAAKAVAfgEALENN---FKMYQQQVVKNAKVLAETLINEGFRIV---SGG 307
Cdd:cd00609 214 GYLIAPPEELLERLKKLLPYTTSGP--STLSQAAAA--AALDDGeehLEELRERYRRRRDALLEALKELGPLVVvkpSGG 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612660568 308 tdNHLVavdVKGSIGLTGKEAEETLDSVGITCNKNTIPFDQEKPFVtsgiRLGTpaattrGFDEKAFEEVAKII 381
Cdd:cd00609 290 --FFLW---LDLPEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGFV----RLSF------ATPEEELEEALERL 348
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
182-337 |
6.13e-05 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 44.68 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 182 KFKEIADEVNAKLMVDMAHI-AGLVAAGLHP-NPVEYADFVTTTTHKTLRGPRGGMILCKEEY---KKDIDKTIFPGI-Q 255
Cdd:PLN02721 162 KVGELAKRHGLKLHIDGARIfNASVALGVPVhRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFirkAKRLRKTLGGGMrQ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 256 GGplehVIAAKAVafgEALENNF-KMYQQQvvKNAKVLAETL-INEGFRIVSGGTDNHLVAVDVKGSIGLTGKEAEETLD 333
Cdd:PLN02721 242 VG----VLAAAAL---VALQENVpKLEDDH--KKAKLLAEGLnQIKGLRVNVAAVETNIVYFDITDGSRITAEKLCKSLE 312
|
....
gi 612660568 334 SVGI 337
Cdd:PLN02721 313 EHGV 316
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
146-241 |
2.12e-04 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 43.20 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 146 DTERINYDEVRKLaLEHKPKLI-VAGASAYSRTI-DFKKFKEIADEVNAKLMVDMAHIAGLVAAGLHPnpvEYADFVTTT 223
Cdd:COG0520 138 EDGELDLEALEAL-LTPRTKLVaVTHVSNVTGTVnPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQA---LGCDFYAFS 213
|
90
....*....|....*....
gi 612660568 224 THKtLRGPRG-GMILCKEE 241
Cdd:COG0520 214 GHK-LYGPTGiGVLYGKRE 231
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
156-243 |
2.69e-04 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 42.55 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 156 RKLALEHKPKLIVAgASAYSRTIDF---KKFKEIADEVNAKLMVDMAHIAGLV---AAGLHPNPVEYA--DFVTTTTHKT 227
Cdd:cd06454 125 REARRPYGKKLIVT-EGVYSMDGDIaplPELVDLAKKYGAILFVDEAHSVGVYgphGRGVEEFGGLTDdvDIIMGTLGKA 203
|
90
....*....|....*.
gi 612660568 228 LrGPRGGMILCKEEYK 243
Cdd:cd06454 204 F-GAVGGYIAGSKELI 218
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
76-296 |
4.06e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 41.82 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 76 DRAKALFGAEHVnVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGAPVNFSGKFynfveyGVDKDTERINY--- 152
Cdd:pfam01212 39 DRVAELFGKEAA-LFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETGGHAELGGVQ------PRPLDGDEAGNmdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 153 DEVRKLALEH------KPKLIV-------AGASAYSrtID-FKKFKEIADEVNAKLMVDMAHIA-GLVAAGLHPNPV-EY 216
Cdd:pfam01212 112 EDLEAAIREVgadifpPTGLISlenthnsAGGQVVS--LEnLREIAALAREHGIPVHLDGARFAnAAVALGVIVKEItSY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612660568 217 ADFVTTTTHKTLRGPRGGMILCKEEYkkdIDKTI-FPGIQGGPLEH--VIAAKAVAfgeALENNFKMYQQQvVKNAKVLA 293
Cdd:pfam01212 190 ADSVTMCLSKGLGAPVGSVLAGSDDF---IAKAIrQRKYLGGGLRQagVLAAAGLR---ALEEGVARLARD-HATARRLA 262
|
...
gi 612660568 294 ETL 296
Cdd:pfam01212 263 EGL 265
|
|
| |
