|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02414 |
PLN02414 |
glycine dehydrogenase (decarboxylating) |
56-1014 |
0e+00 |
|
glycine dehydrogenase (decarboxylating)
Pssm-ID: 178035 [Multi-domain] Cd Length: 993 Bit Score: 1500.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 56 RLLERLLPRH------------DDFSRRHIGPGDKDRREMLQALGLASIDELIEKTVPASIRlKRPLKME---DPICENE 120
Cdd:PLN02414 11 GLLRRLVNEQtrsisvealkpsDTFPRRHNSATPEEQKAMAEYCGFDSLDALIDATVPKSIR-LDSMKLSkydEGLTESQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 121 ILETLHAIASKNQIWRSYIGMGYYNCSVPQTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANAS 200
Cdd:PLN02414 90 MLEHMKSLASKNKVFKSYIGMGYYNTHVPPVILRNILENPGWYTQYTPYQAEIAQGRLESLLNYQTMITDLTGLPMSNAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 201 LLDEATAAAEAMQLCHRHN--KRKKFFVDPRCHPQTIAVVQTRAKYRGVLVELKLPHEMDFSGKDVCGVLFQYPDTEGKV 278
Cdd:PLN02414 170 LLDEGTAAAEAMAMCNNILkgKKKKFLIASNCHPQTIDVCQTRADGLGLEVVVADEKDFDYSSGDVCGVLVQYPATDGEV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 279 EDFTELVDRAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVKENLVRMMPGRMVGVTR 358
Cdd:PLN02414 250 LDYAEFVKNAHANGVKVVMATDLLALTMLKPPGEWGADIVVGSAQRFGVPMGYGGPHAAFLATSQEYKRLMPGRIIGVSV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 359 DATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSQGLKHIAKRVHNATLILSEGLKRAGHQLQHDL 438
Cdd:PLN02414 330 DSSGKPALRMAMQTREQHIRRDKATSNICTAQALLANMAAMYAVYHGPEGLKTIAQRVHGLAGVFAAGLKKLGFQVQSLP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 439 FFDTLKVQCGcSVKEVLGRAAQRQINFRLFDDGTLGISLDETVTEKDLDDLLWIFGCESSAELVAEGMGEERRGLLGSSF 518
Cdd:PLN02414 410 FFDTVKVKCS-DADAIADAAAKVGINLRVVDANTVTVSFDETTTLEDVDKLFKVFAGGKPVPFTAESLAPEVDSSIPSSL 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 519 KRTSPFLTHQVFNSYHSETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELAPITWREFANIHPFVPLDQAQGYQQ 598
Cdd:PLN02414 489 ARESPYLTHPIFNQYHSEHELLRYLHRLQNKDLSLVHSMIPLGSCTMKLNATTEMMPVTWPEFANIHPFAPVDQAQGYQE 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 599 LFQGLEKDLCEITGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAHMAGMKIQPVEVDRY 678
Cdd:PLN02414 569 MFEDLGDLLCEITGFDSFSLQPNAGAAGEYAGLMVIRAYHLSRGDHHRNVCIIPVSAHGTNPASAAMCGMKIVVVGTDAK 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 679 GNIDVAHLKAMVDQHKENLAAIMITYPSTNGVFEENIGDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLH 758
Cdd:PLN02414 649 GNINIEELRKAAEAHKDNLAALMVTYPSTHGVYEEGIDEICDIIHDNGGQVYMDGANMNAQVGLTSPGFIGADVCHLNLH 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 759 KTFCIPHGGGGPGMGPIGVKKHLSPFLPSHPVI---SIKPTEGTWPVGTVSAAPWGSSSILPISWAYIKMMGGKGLKEAT 835
Cdd:PLN02414 729 KTFCIPHGGGGPGMGPIGVKKHLAPFLPSHPVVptgGIPRPEKTQPLGTISAAPWGSALILPISYTYIAMMGSEGLTDAS 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 836 EIAILNANYMAKRLEKHYRVLFRGARGYVAHEFILDTRPFKKSANVEAVDVAKRLQDYGFHAPTMSWPVAGTLMIEPTES 915
Cdd:PLN02414 809 KIAILNANYMAKRLEGHYPVLFRGKNGTCAHEFIIDLRPFKNTAGIEPEDVAKRLMDYGFHAPTMSWPVPGTLMIEPTES 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 916 EDKAELDRFCDAMISIRQEIADIEEGRIDPRVNPLKMSPHSLTCVTSSCWDRPYSREVAAFPLPFVKpENKFWPTIARID 995
Cdd:PLN02414 889 ESKAELDRFCDALISIREEIADIENGKADRENNVLKGAPHPPSLLMADKWDKPYSREYAAFPAPWVR-ASKFWPTTGRVD 967
|
970
....*....|....*....
gi 20070408 996 DIYGDQHLVCTCPPMEVYE 1014
Cdd:PLN02414 968 NVYGDRNLVCTLPSAAEEE 986
|
|
| gcvP |
TIGR00461 |
glycine dehydrogenase (decarboxylating); This apparently ubiquitous enzyme is found in ... |
71-1007 |
0e+00 |
|
glycine dehydrogenase (decarboxylating); This apparently ubiquitous enzyme is found in bacterial, mammalian and plant sources. The enzyme catalyzes the reaction: GLYCINE + LIPOYLPROTEIN = S-AMINOMETHYL-DIHYDROLIPOYLPROTEIN + CO2. It is part of the glycine decarboxylase multienzyme complex (GDC) consisting of four proteins P, H, L and T. Active site in E.coli is located as the (K) residues at position 713 of the SEED alignment. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273089 [Multi-domain] Cd Length: 939 Bit Score: 1320.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 71 RHIGPGDKDRREMLQALGLASIDELIEKTVPASIRLKRPLKMEDPICENEILETLHAIASKNQIWRSYIGMGYYNCSVPQ 150
Cdd:TIGR00461 1 RHLGPGETEQRQMLQTLGFDTLNALIDQAVPPAIRFPRPLQLPAPQSEYGALAQLKSIASKNQVFRSYIGMGYYDTILPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 151 TILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRK--KFFVDP 228
Cdd:TIGR00461 81 VIQRNILENPGWYTAYTPYQPEISQGRLEALLNFQTVVMDLTGLEIANASLLDEGTAAAEAMALSYGVSKSKanAFFVAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 229 RCHPQTIAVVQTRAKYRGVLVELKLPHEMDFSgKDVCGVLFQYPDTEGKVEDFTELVDRAHQTGSLTCCATDLLALCILR 308
Cdd:TIGR00461 161 DCHPQTIEVIKTRANPFGIEVIVGDHHTFSFS-TDVFGALLQYPATDGAIYDYRSLIDKLHSHKALVSVAADPMALTLLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 309 PPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVKENLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICT 388
Cdd:TIGR00461 240 PPGELGADIVVGSTQRFGVPMGYGGPHAAFFATKDEYQRKMPGRIVGVSKDAHGNTALRLALQTREQHIRRDKATSNICT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 389 AQALLANMAAMFAIYHGSQGLKHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCG-CSVKEVLGRAAQRQINFRL 467
Cdd:TIGR00461 320 AQVLLANMASMYGVYHGPTGLKNIALRIHQLTVILAIGLKRLNYSLNNDYFFDTLRVGVGeQSAPAILKAAEGRGINLRP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 468 FDDGTLGISLDETVTEKDLDDLLWIFGCESSAELVAEGMGEERRGLLGSSFKRTSPFLTHQVFNSYHSETNLVRYMKKLE 547
Cdd:TIGR00461 400 LVPGEVGISLDETTTVQDVLDLWQVFAGKDNLPFTPEELWSDVKTSFPADLTRQDEILQDAVFNQYHSETEMLRYLHQLE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 548 NKDISLVHSMIPLGSCTMKLNSSSELAPITWREFANIHPFVPLDQAQGYQQLFQGLEKDLCEITGYDRVSFQPNSGAQGE 627
Cdd:TIGR00461 480 SKDLALNTSMIPLGSCTMKLNATAEMMPITWPEFGKIHPFAPAGQTEGYQILIAQLEAWLGEITGFDAISLQPNSGAQGE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 628 YAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAHMAGMKIQPVEVDRYGNIDVAHLKAMVDQHKENLAAIMITYPST 707
Cdd:TIGR00461 560 YAGLQVIRQYHESRGEEHRNICLIPESAHGTNPASAVMAGMQVVPVKCDGEGNIDLEDLTSKAEQYGDRLAALMVTYPST 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 708 NGVFEENIGDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLSPFLPS 787
Cdd:TIGR00461 640 HGVFEATIGTICDIVHRFGGQVYLDGANMNAQVGLTSPGDFGADVCHLNLHKTFCIPHGGGGPGMGPIGVKSHLQPFLPR 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 788 HPVISIKPTEG-TWPVGTVSAAPWGSSSILPISWAYIKMMGGKGLKEATEIAILNANYMAKRLEKHYRVLFRGARGYVAH 866
Cdd:TIGR00461 720 HSLNSTAELQGeDQSIGMVSAAPYGSASILPISWMYIAMMGPEGLTKASEVAILNANYMAKRLEDYYPILFRGNNELVAH 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 867 EFILDTRPFKKSANVEAVDVAKRLQDYGFHAPTMSWPVAGTLMIEPTESEDKAELDRFCDAMISIRQEIADIEEGRIDPR 946
Cdd:TIGR00461 800 ECILDLRPLKKQAGIEVEDVAKRLMDYGFHAPTVSFPVLGTLMVEPTESESLGELDRFCDAMIAIYQEIQAITAGEIDPA 879
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20070408 947 VNPLKMSPHSLTCVTSSCWDRPYSREVAAFPLPFVKpENKFWPTIARIDDIYGDQHLVCTC 1007
Cdd:TIGR00461 880 DNPLKNAPHTAQSLICGEWNHPYSREEAAYPAPWTK-QFKFWPTVGRLDDTYGDRNLVCSC 939
|
|
| GDC-P |
pfam02347 |
Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins ... |
70-493 |
0e+00 |
|
Glycine cleavage system P-protein; 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 catalyzed by this protein is:- Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2
Pssm-ID: 396772 [Multi-domain] Cd Length: 428 Bit Score: 766.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 70 RRHIGPGDKDRREMLQALGLASIDELIEKTVPASIRLKRPLKMEDPICENEILETLHAIASKNQIWRSYIGMGYYNCSVP 149
Cdd:pfam02347 1 DRHIGPSEKDQQEMLATLGYSSLDDLIGKAVPKNIRFAKPLQLPAPKSEYEALAELEAIASKNTVYRSFIGMGYYDTILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 150 QTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRK--KFFVD 227
Cdd:pfam02347 81 PVILRNILENPEWYTAYTPYQPEISQGRLEALLNFQTMICDLTGLDIANASLLDEGTAAAEAMALAARASKKKgkKFVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 228 PRCHPQTIAVVQTRAKYRGVLVELKLPHEMDFSG-KDVCGVLFQYPDTEGKVEDFTELVDRAHQTGSLTCCATDLLALCI 306
Cdd:pfam02347 161 KDVHPQTLEVLKTRAKPFGIEIVEVDYTEEGVTDlKDVFGVLVQYPNTDGRIEDYKELIELAHQRKSLVVVAADLLALTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 307 LRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVKENLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNI 386
Cdd:pfam02347 241 LKPPGEFGADIAVGSAQRFGVPLGYGGPHAGFFAVKKELVRKMPGRLVGVSKDANGKRALRLALQTREQHIRRDKATSNI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 387 CTAQALLANMAAMFAIYHGSQGLKHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCG-CSVKEVLGRAAQRQINF 465
Cdd:pfam02347 321 CTAQALLANMASMYAVYHGPNGLKEIARRIHSLTLYLAKALKKLGHELVHKHFFDTLLIEVEdKAVEEVLARAEARGINL 400
|
410 420
....*....|....*....|....*...
gi 20070408 466 RLFDDGTLGISLDETVTEKDLDDLLWIF 493
Cdd:pfam02347 401 RYVDLGHVGIALDETVTKEDIDDLLQVF 428
|
|
| GcvP2 |
COG1003 |
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ... |
513-1006 |
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: 741.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 513 LLGSSFKRTSPflthqVFNSYHSETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELAPITWREFANIHPFVPLDQ 592
Cdd:COG1003 13 LLPEALLRKSP-----VFLPEVSETEVLRHYTRLSQKNLGLDTGMIPLGSCTMKYNPKINEEPATLPGFANLHPFQPEET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 593 AQGYQQLFQGLEKDLCEITGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAHMAGMKIQP 672
Cdd:COG1003 88 VQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGEGHRNEILIPDSAHGTNPASAAMAGFKVVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 673 VEVDRYGNIDVAHLKAMVDqhkENLAAIMITYPSTNGVFEENIGDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDV 752
Cdd:COG1003 168 VKSDEDGNVDLEDLKAKVG---DRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARPGDMGFDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 753 SHLNLHKTFCIphggggpgmgpigVKKHLSPFLPSHPVIsikPTEGTWPVGT-------VSAAPWGSSSILPISWAYIKM 825
Cdd:COG1003 245 CHLNLHKTFSTphggggpgsgpvgVKEHLAPFLPGPPVV---KDGDKYRLDYdrpksigRSAAFYGNAGVLVRAYAYIRM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 826 MGGKGLKEATEIAILNANYMAKRLEKHYRVLFRGaRGYVAHEFILDTRPFKKSANVEAVDVAKRLQDYGFHAPTMSWP-- 903
Cdd:COG1003 322 MGAEGLREATEVAVLNANYLAARLKDHYPVLYTG-NGRCAHEFILDLRPLKKETGVTTLDIAKRLLDYGFHAPTMYFPli 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 904 VAGTLMIEPTESEDKAELDRFCDAMISIRQEIADieegriDPrvNPLKMSPHSLtcvtsscwdrpysrevaafplpfvkp 983
Cdd:COG1003 401 VPETLMIEPTESESKEELDRFIDAMIAIREEARE------DP--EPLKNAPHTT-------------------------- 446
|
490 500
....*....|....*....|...
gi 20070408 984 enkfwpTIARIDDIYGDQHLVCT 1006
Cdd:COG1003 447 ------PVRRLDEVYADRNLVLT 463
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
118-493 |
3.36e-176 |
|
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: 519.10 E-value: 3.36e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 118 ENEILETLHAIASKNQIWR---SYIGMGYYNCSVPQTILRNLLENsGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGL 194
Cdd:cd00613 1 ETEVLRHLKRLASKNKALDqsmSFLGSGTYKHNPPAVIKRNILEN-EFYTAYTPYQPEISQGRLQALFELQTMLCELTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 195 DMANASLLDEATAAAEAMQLCHRHNK--RKKFFVDPRCHPQTIAVVQTRAKYRGVLVELKLPHEM---------DFSGKD 263
Cdd:cd00613 80 DVANASLQDEATAAAEAAGLAAIRAYhkRNKVLVPDSAHPTNPAVARTRGEPLGIEVVEVPSDEGgtvdlealkEEVSEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 264 VCGVLFQYPDTEGKVEDF-TELVDRAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVK 342
Cdd:cd00613 160 VAALMVQYPNTLGVFEDLiKEIADIAHSAGALVYVDGDNLNLTGLKPPGEYGADIVVGNLQKTGVPHGGGGPGAGFFAVK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 343 ENLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSQGLKHIAKRVHNATLI 422
Cdd:cd00613 240 KELVRFLPGRLVGVTKDAEGNRAFRLALQTREQHIRREKATSNICTGQALLALMAAMYIVYLGPEGLKEIAERAHLNANY 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20070408 423 LSEGLKRAGHQLQ-HDLFFDTLKVQCGC---SVKEVLGRAAQRQINFR----LFDDGTLGISLDETVTEKDLDDLLWIF 493
Cdd:cd00613 320 LAKRLKEVGGVLPfNGPFFHEFVLRLPPlygIRAEDLAKALIDGGFHAptmyLPVDGTLMIEPTETETKEELDALLEAL 398
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02414 |
PLN02414 |
glycine dehydrogenase (decarboxylating) |
56-1014 |
0e+00 |
|
glycine dehydrogenase (decarboxylating)
Pssm-ID: 178035 [Multi-domain] Cd Length: 993 Bit Score: 1500.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 56 RLLERLLPRH------------DDFSRRHIGPGDKDRREMLQALGLASIDELIEKTVPASIRlKRPLKME---DPICENE 120
Cdd:PLN02414 11 GLLRRLVNEQtrsisvealkpsDTFPRRHNSATPEEQKAMAEYCGFDSLDALIDATVPKSIR-LDSMKLSkydEGLTESQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 121 ILETLHAIASKNQIWRSYIGMGYYNCSVPQTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANAS 200
Cdd:PLN02414 90 MLEHMKSLASKNKVFKSYIGMGYYNTHVPPVILRNILENPGWYTQYTPYQAEIAQGRLESLLNYQTMITDLTGLPMSNAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 201 LLDEATAAAEAMQLCHRHN--KRKKFFVDPRCHPQTIAVVQTRAKYRGVLVELKLPHEMDFSGKDVCGVLFQYPDTEGKV 278
Cdd:PLN02414 170 LLDEGTAAAEAMAMCNNILkgKKKKFLIASNCHPQTIDVCQTRADGLGLEVVVADEKDFDYSSGDVCGVLVQYPATDGEV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 279 EDFTELVDRAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVKENLVRMMPGRMVGVTR 358
Cdd:PLN02414 250 LDYAEFVKNAHANGVKVVMATDLLALTMLKPPGEWGADIVVGSAQRFGVPMGYGGPHAAFLATSQEYKRLMPGRIIGVSV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 359 DATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSQGLKHIAKRVHNATLILSEGLKRAGHQLQHDL 438
Cdd:PLN02414 330 DSSGKPALRMAMQTREQHIRRDKATSNICTAQALLANMAAMYAVYHGPEGLKTIAQRVHGLAGVFAAGLKKLGFQVQSLP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 439 FFDTLKVQCGcSVKEVLGRAAQRQINFRLFDDGTLGISLDETVTEKDLDDLLWIFGCESSAELVAEGMGEERRGLLGSSF 518
Cdd:PLN02414 410 FFDTVKVKCS-DADAIADAAAKVGINLRVVDANTVTVSFDETTTLEDVDKLFKVFAGGKPVPFTAESLAPEVDSSIPSSL 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 519 KRTSPFLTHQVFNSYHSETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELAPITWREFANIHPFVPLDQAQGYQQ 598
Cdd:PLN02414 489 ARESPYLTHPIFNQYHSEHELLRYLHRLQNKDLSLVHSMIPLGSCTMKLNATTEMMPVTWPEFANIHPFAPVDQAQGYQE 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 599 LFQGLEKDLCEITGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAHMAGMKIQPVEVDRY 678
Cdd:PLN02414 569 MFEDLGDLLCEITGFDSFSLQPNAGAAGEYAGLMVIRAYHLSRGDHHRNVCIIPVSAHGTNPASAAMCGMKIVVVGTDAK 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 679 GNIDVAHLKAMVDQHKENLAAIMITYPSTNGVFEENIGDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLH 758
Cdd:PLN02414 649 GNINIEELRKAAEAHKDNLAALMVTYPSTHGVYEEGIDEICDIIHDNGGQVYMDGANMNAQVGLTSPGFIGADVCHLNLH 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 759 KTFCIPHGGGGPGMGPIGVKKHLSPFLPSHPVI---SIKPTEGTWPVGTVSAAPWGSSSILPISWAYIKMMGGKGLKEAT 835
Cdd:PLN02414 729 KTFCIPHGGGGPGMGPIGVKKHLAPFLPSHPVVptgGIPRPEKTQPLGTISAAPWGSALILPISYTYIAMMGSEGLTDAS 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 836 EIAILNANYMAKRLEKHYRVLFRGARGYVAHEFILDTRPFKKSANVEAVDVAKRLQDYGFHAPTMSWPVAGTLMIEPTES 915
Cdd:PLN02414 809 KIAILNANYMAKRLEGHYPVLFRGKNGTCAHEFIIDLRPFKNTAGIEPEDVAKRLMDYGFHAPTMSWPVPGTLMIEPTES 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 916 EDKAELDRFCDAMISIRQEIADIEEGRIDPRVNPLKMSPHSLTCVTSSCWDRPYSREVAAFPLPFVKpENKFWPTIARID 995
Cdd:PLN02414 889 ESKAELDRFCDALISIREEIADIENGKADRENNVLKGAPHPPSLLMADKWDKPYSREYAAFPAPWVR-ASKFWPTTGRVD 967
|
970
....*....|....*....
gi 20070408 996 DIYGDQHLVCTCPPMEVYE 1014
Cdd:PLN02414 968 NVYGDRNLVCTLPSAAEEE 986
|
|
| gcvP |
TIGR00461 |
glycine dehydrogenase (decarboxylating); This apparently ubiquitous enzyme is found in ... |
71-1007 |
0e+00 |
|
glycine dehydrogenase (decarboxylating); This apparently ubiquitous enzyme is found in bacterial, mammalian and plant sources. The enzyme catalyzes the reaction: GLYCINE + LIPOYLPROTEIN = S-AMINOMETHYL-DIHYDROLIPOYLPROTEIN + CO2. It is part of the glycine decarboxylase multienzyme complex (GDC) consisting of four proteins P, H, L and T. Active site in E.coli is located as the (K) residues at position 713 of the SEED alignment. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273089 [Multi-domain] Cd Length: 939 Bit Score: 1320.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 71 RHIGPGDKDRREMLQALGLASIDELIEKTVPASIRLKRPLKMEDPICENEILETLHAIASKNQIWRSYIGMGYYNCSVPQ 150
Cdd:TIGR00461 1 RHLGPGETEQRQMLQTLGFDTLNALIDQAVPPAIRFPRPLQLPAPQSEYGALAQLKSIASKNQVFRSYIGMGYYDTILPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 151 TILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRK--KFFVDP 228
Cdd:TIGR00461 81 VIQRNILENPGWYTAYTPYQPEISQGRLEALLNFQTVVMDLTGLEIANASLLDEGTAAAEAMALSYGVSKSKanAFFVAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 229 RCHPQTIAVVQTRAKYRGVLVELKLPHEMDFSgKDVCGVLFQYPDTEGKVEDFTELVDRAHQTGSLTCCATDLLALCILR 308
Cdd:TIGR00461 161 DCHPQTIEVIKTRANPFGIEVIVGDHHTFSFS-TDVFGALLQYPATDGAIYDYRSLIDKLHSHKALVSVAADPMALTLLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 309 PPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVKENLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICT 388
Cdd:TIGR00461 240 PPGELGADIVVGSTQRFGVPMGYGGPHAAFFATKDEYQRKMPGRIVGVSKDAHGNTALRLALQTREQHIRRDKATSNICT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 389 AQALLANMAAMFAIYHGSQGLKHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCG-CSVKEVLGRAAQRQINFRL 467
Cdd:TIGR00461 320 AQVLLANMASMYGVYHGPTGLKNIALRIHQLTVILAIGLKRLNYSLNNDYFFDTLRVGVGeQSAPAILKAAEGRGINLRP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 468 FDDGTLGISLDETVTEKDLDDLLWIFGCESSAELVAEGMGEERRGLLGSSFKRTSPFLTHQVFNSYHSETNLVRYMKKLE 547
Cdd:TIGR00461 400 LVPGEVGISLDETTTVQDVLDLWQVFAGKDNLPFTPEELWSDVKTSFPADLTRQDEILQDAVFNQYHSETEMLRYLHQLE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 548 NKDISLVHSMIPLGSCTMKLNSSSELAPITWREFANIHPFVPLDQAQGYQQLFQGLEKDLCEITGYDRVSFQPNSGAQGE 627
Cdd:TIGR00461 480 SKDLALNTSMIPLGSCTMKLNATAEMMPITWPEFGKIHPFAPAGQTEGYQILIAQLEAWLGEITGFDAISLQPNSGAQGE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 628 YAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAHMAGMKIQPVEVDRYGNIDVAHLKAMVDQHKENLAAIMITYPST 707
Cdd:TIGR00461 560 YAGLQVIRQYHESRGEEHRNICLIPESAHGTNPASAVMAGMQVVPVKCDGEGNIDLEDLTSKAEQYGDRLAALMVTYPST 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 708 NGVFEENIGDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLSPFLPS 787
Cdd:TIGR00461 640 HGVFEATIGTICDIVHRFGGQVYLDGANMNAQVGLTSPGDFGADVCHLNLHKTFCIPHGGGGPGMGPIGVKSHLQPFLPR 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 788 HPVISIKPTEG-TWPVGTVSAAPWGSSSILPISWAYIKMMGGKGLKEATEIAILNANYMAKRLEKHYRVLFRGARGYVAH 866
Cdd:TIGR00461 720 HSLNSTAELQGeDQSIGMVSAAPYGSASILPISWMYIAMMGPEGLTKASEVAILNANYMAKRLEDYYPILFRGNNELVAH 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 867 EFILDTRPFKKSANVEAVDVAKRLQDYGFHAPTMSWPVAGTLMIEPTESEDKAELDRFCDAMISIRQEIADIEEGRIDPR 946
Cdd:TIGR00461 800 ECILDLRPLKKQAGIEVEDVAKRLMDYGFHAPTVSFPVLGTLMVEPTESESLGELDRFCDAMIAIYQEIQAITAGEIDPA 879
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20070408 947 VNPLKMSPHSLTCVTSSCWDRPYSREVAAFPLPFVKpENKFWPTIARIDDIYGDQHLVCTC 1007
Cdd:TIGR00461 880 DNPLKNAPHTAQSLICGEWNHPYSREEAAYPAPWTK-QFKFWPTVGRLDDTYGDRNLVCSC 939
|
|
| GDC-P |
pfam02347 |
Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins ... |
70-493 |
0e+00 |
|
Glycine cleavage system P-protein; 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 catalyzed by this protein is:- Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2
Pssm-ID: 396772 [Multi-domain] Cd Length: 428 Bit Score: 766.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 70 RRHIGPGDKDRREMLQALGLASIDELIEKTVPASIRLKRPLKMEDPICENEILETLHAIASKNQIWRSYIGMGYYNCSVP 149
Cdd:pfam02347 1 DRHIGPSEKDQQEMLATLGYSSLDDLIGKAVPKNIRFAKPLQLPAPKSEYEALAELEAIASKNTVYRSFIGMGYYDTILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 150 QTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRK--KFFVD 227
Cdd:pfam02347 81 PVILRNILENPEWYTAYTPYQPEISQGRLEALLNFQTMICDLTGLDIANASLLDEGTAAAEAMALAARASKKKgkKFVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 228 PRCHPQTIAVVQTRAKYRGVLVELKLPHEMDFSG-KDVCGVLFQYPDTEGKVEDFTELVDRAHQTGSLTCCATDLLALCI 306
Cdd:pfam02347 161 KDVHPQTLEVLKTRAKPFGIEIVEVDYTEEGVTDlKDVFGVLVQYPNTDGRIEDYKELIELAHQRKSLVVVAADLLALTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 307 LRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVKENLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNI 386
Cdd:pfam02347 241 LKPPGEFGADIAVGSAQRFGVPLGYGGPHAGFFAVKKELVRKMPGRLVGVSKDANGKRALRLALQTREQHIRRDKATSNI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 387 CTAQALLANMAAMFAIYHGSQGLKHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCG-CSVKEVLGRAAQRQINF 465
Cdd:pfam02347 321 CTAQALLANMASMYAVYHGPNGLKEIARRIHSLTLYLAKALKKLGHELVHKHFFDTLLIEVEdKAVEEVLARAEARGINL 400
|
410 420
....*....|....*....|....*...
gi 20070408 466 RLFDDGTLGISLDETVTEKDLDDLLWIF 493
Cdd:pfam02347 401 RYVDLGHVGIALDETVTKEDIDDLLQVF 428
|
|
| GcvP2 |
COG1003 |
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ... |
513-1006 |
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: 741.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 513 LLGSSFKRTSPflthqVFNSYHSETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELAPITWREFANIHPFVPLDQ 592
Cdd:COG1003 13 LLPEALLRKSP-----VFLPEVSETEVLRHYTRLSQKNLGLDTGMIPLGSCTMKYNPKINEEPATLPGFANLHPFQPEET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 593 AQGYQQLFQGLEKDLCEITGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAHMAGMKIQP 672
Cdd:COG1003 88 VQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGEGHRNEILIPDSAHGTNPASAAMAGFKVVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 673 VEVDRYGNIDVAHLKAMVDqhkENLAAIMITYPSTNGVFEENIGDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDV 752
Cdd:COG1003 168 VKSDEDGNVDLEDLKAKVG---DRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARPGDMGFDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 753 SHLNLHKTFCIphggggpgmgpigVKKHLSPFLPSHPVIsikPTEGTWPVGT-------VSAAPWGSSSILPISWAYIKM 825
Cdd:COG1003 245 CHLNLHKTFSTphggggpgsgpvgVKEHLAPFLPGPPVV---KDGDKYRLDYdrpksigRSAAFYGNAGVLVRAYAYIRM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 826 MGGKGLKEATEIAILNANYMAKRLEKHYRVLFRGaRGYVAHEFILDTRPFKKSANVEAVDVAKRLQDYGFHAPTMSWP-- 903
Cdd:COG1003 322 MGAEGLREATEVAVLNANYLAARLKDHYPVLYTG-NGRCAHEFILDLRPLKKETGVTTLDIAKRLLDYGFHAPTMYFPli 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 904 VAGTLMIEPTESEDKAELDRFCDAMISIRQEIADieegriDPrvNPLKMSPHSLtcvtsscwdrpysrevaafplpfvkp 983
Cdd:COG1003 401 VPETLMIEPTESESKEELDRFIDAMIAIREEARE------DP--EPLKNAPHTT-------------------------- 446
|
490 500
....*....|....*....|...
gi 20070408 984 enkfwpTIARIDDIYGDQHLVCT 1006
Cdd:COG1003 447 ------PVRRLDEVYADRNLVLT 463
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
66-494 |
0e+00 |
|
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: 659.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 66 DDFSRRHIGPGDKDRREMLQALGLASIDELIEKtVPASIRLKRPLKMEDPICENEILETLHAIASKNQIWRSYIGMGYYN 145
Cdd:COG0403 1 DEFAMRYIPPTEEDRAEMLAAIGVDSLDELFDD-IPAEIRLKRPLDLPEALSEAELLRHLRALAAKNKVLTSFIGAGYYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 146 CSVPQTIlRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKR-KKF 224
Cdd:COG0403 80 HYVPAVV-RNILERPEFYTAYTPYQPEISQGRLQALFEFQTMVAELTGMDVANASLYDGATAAAEAMLMARRVTKRsNKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 225 FVDPRCHPQTIAVVQTRAKYRGV-LVELKLPH-EMDFS------GKDVCGVLFQYPDTEGKVEDFTELVDRAHQTGSLTC 296
Cdd:COG0403 159 LVSEDVHPQTRAVLKTYAEPLGIeVVEVPDEDgVTDLEalkallDDDVAGVLVQYPNFFGVIEDLRAIAEAAHAAGALVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 297 CATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVKENLVRMMPGRMVGVTRDATGKEVYRLALQTREQH 376
Cdd:COG0403 239 VAADPLSLGLLKPPGELGADIVVGEGQRLGVPLGFGGPHAGFFATREKLVRQMPGRLVGVTVDADGKRAFRLTLQTREQH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 377 IRRDKATSNICTAQALLANMAAMFAIYHGSQGLKHIAKRVHNATLILSEGLKRAGHQLQ-HDLFFDTLKVQCGCSVKEVL 455
Cdd:COG0403 319 IRREKATSNICTNQALLALAASMYAVYHGPEGLKEIAERIHQKAHYLAERLAALGVEVPfNGPFFDEFVVRLPKPAAEIN 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 20070408 456 GRAAQRQI----NFRLFDDGTLGISLDETVTEKDLDDLLWIFG 494
Cdd:COG0403 399 AALLEKGIlgglNLRRVDDDTLLVAVTETTTKEDIDALVEALA 441
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
118-493 |
3.36e-176 |
|
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: 519.10 E-value: 3.36e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 118 ENEILETLHAIASKNQIWR---SYIGMGYYNCSVPQTILRNLLENsGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGL 194
Cdd:cd00613 1 ETEVLRHLKRLASKNKALDqsmSFLGSGTYKHNPPAVIKRNILEN-EFYTAYTPYQPEISQGRLQALFELQTMLCELTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 195 DMANASLLDEATAAAEAMQLCHRHNK--RKKFFVDPRCHPQTIAVVQTRAKYRGVLVELKLPHEM---------DFSGKD 263
Cdd:cd00613 80 DVANASLQDEATAAAEAAGLAAIRAYhkRNKVLVPDSAHPTNPAVARTRGEPLGIEVVEVPSDEGgtvdlealkEEVSEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 264 VCGVLFQYPDTEGKVEDF-TELVDRAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVK 342
Cdd:cd00613 160 VAALMVQYPNTLGVFEDLiKEIADIAHSAGALVYVDGDNLNLTGLKPPGEYGADIVVGNLQKTGVPHGGGGPGAGFFAVK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 343 ENLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSQGLKHIAKRVHNATLI 422
Cdd:cd00613 240 KELVRFLPGRLVGVTKDAEGNRAFRLALQTREQHIRREKATSNICTGQALLALMAAMYIVYLGPEGLKEIAERAHLNANY 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20070408 423 LSEGLKRAGHQLQ-HDLFFDTLKVQCGC---SVKEVLGRAAQRQINFR----LFDDGTLGISLDETVTEKDLDDLLWIF 493
Cdd:cd00613 320 LAKRLKEVGGVLPfNGPFFHEFVLRLPPlygIRAEDLAKALIDGGFHAptmyLPVDGTLMIEPTETETKEELDALLEAL 398
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
536-928 |
1.41e-158 |
|
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: 473.64 E-value: 1.41e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 536 ETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELAPITWR-EFANIHPFVPLDQAQGYQQLFQGLEKDLCEITGYD 614
Cdd:cd00613 1 ETEVLRHLKRLASKNKALDQSMSFLGSGTYKHNPPAVIKRNILEnEFYTAYTPYQPEISQGRLQALFELQTMLCELTGMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 615 --RVSFQPNSGAQGEYAGLATIRAYLdqkgerHRTVCLIPKSAHGTNPASAHMA----GMKIQPVEVDRYGNIDvahLKA 688
Cdd:cd00613 81 vaNASLQDEATAAAEAAGLAAIRAYH------KRNKVLVPDSAHPTNPAVARTRgeplGIEVVEVPSDEGGTVD---LEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 689 MVDQHKENLAAIMITYPSTNGVFEENIGDVCALIHQHGGQVYLDGANMNAQvGICRPGDFGSDVSHLNLHKTF------- 761
Cdd:cd00613 152 LKEEVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNLT-GLKPPGEYGADIVVGNLQKTGvphgggg 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 762 ------CiphggggpgmgpigVKKHLSPFLPSHPVISIKPTEGTwPVGTVSAA---------------PWGSSSILPISW 820
Cdd:cd00613 231 pgagffA--------------VKKELVRFLPGRLVGVTKDAEGN-RAFRLALQtreqhirrekatsniCTGQALLALMAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 821 AYIKMMGGKGLKEATEIAILNANYMAKRLEKHYRVLfrGARGYVAHEFILDTRPFkksANVEAVDVAKRLQDYGFHAPTM 900
Cdd:cd00613 296 MYIVYLGPEGLKEIAERAHLNANYLAKRLKEVGGVL--PFNGPFFHEFVLRLPPL---YGIRAEDLAKALIDGGFHAPTM 370
|
410 420
....*....|....*....|....*...
gi 20070408 901 SWPVAGTLMIEPTESEDKAELDRFCDAM 928
Cdd:cd00613 371 YLPVDGTLMIEPTETETKEELDALLEAL 398
|
|
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
535-958 |
2.44e-143 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 437.24 E-value: 2.44e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 535 SETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNssselaP-ITWR-----EFANIHPFVPLDQAQGYQQLFQGLEKDLC 608
Cdd:PRK04366 50 SELEVVRHYTRLSQKNYGVDTGFYPLGSCTMKYN------PkINEKvarlpGFAELHPLQPEETVQGALELMYELQEWLK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 609 EITGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAHMAGMKIQPVEVDRYGNIDVAHLKA 688
Cdd:PRK04366 124 EITGMDAVTLQPAAGAHGELTGLLMIRAYHEARGDTKRTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 689 MVDqhkENLAAIMITYPSTNGVFEENIGDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGG 768
Cdd:PRK04366 204 AVG---EDTAALMLTNPNTLGLFERNILEIAEIVHEAGGLLYYDGANLNAILGKARPGDMGFDVVHLNLHKTFSTPHGGG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 769 GPGMGPIGVKKHLSPFLPsHPVisIKPTEGTW--------PVGTVSAApWGSSSILPISWAYIKMMGGKGLKEATEIAIL 840
Cdd:PRK04366 281 GPGSGPVGVKEELAPFLP-VPV--VEKDGDRYrldydrpkSIGRVRAF-YGNFGVLVRAYAYIRSLGAEGLREVSEDAVL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 841 NANYMAKRLEKHYRVLFRGARgyvAHEFILDTRPFKKSaNVEAVDVAKRLQDYGFHAPTMSWP--VAGTLMIEPTESEDK 918
Cdd:PRK04366 357 NANYLKARLKDIYDLPYDRPC---MHEFVLSGKKLKET-GVRTLDIAKRLLDYGFHPPTIYFPliVPEALMIEPTETESK 432
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 20070408 919 AELDRFCDAMISIRqeiadiEEGRIDPRVnpLKMSPHSLT 958
Cdd:PRK04366 433 ETLDAFIAAMKQIA------EEAKENPEL--VKEAPHNTP 464
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
77-489 |
1.08e-124 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 387.19 E-value: 1.08e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 77 DKDRREMLQALGLASIDELIEKtVPASIRLKRPLKMEDPICENEILETLHAIASKNQIWR---SYIGMGYYNCSVPqTIL 153
Cdd:PRK00451 9 EEDIREMLDAIGVKSIDELFAD-IPEELRLKRPLDLPPGLSEMELLRHLRELAAKNKTAEeypSFLGAGAYDHYIP-AVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 154 RNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRKKFFVDPRCHPQ 233
Cdd:PRK00451 87 DHIISRSEFYTAYTPYQPEISQGTLQAIFEYQTMICELTGMDVANASMYDGATALAEAALMAVRITKRKKVLVSGAVHPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 234 TIAVVQTRAKYRGV-LVELKLPHEM-------DFSGKDVCGVLFQYPDTEGKVEDFTELVDRAHQTGSLTCCATDLLALC 305
Cdd:PRK00451 167 YREVLKTYLKGQGIeVVEVPYEDGVtdlealeAAVDDDTAAVVVQYPNFFGVIEDLEEIAEIAHAGGALFIVGVDPVSLG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 306 ILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVKENLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSN 385
Cdd:PRK00451 247 LLKPPGEYGADIVVGEGQPLGIPLSFGGPYLGFFATRKKLVRQMPGRLVGETVDADGKRGFVLTLQAREQHIRREKATSN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 386 ICTAQALLANMAAMFAIYHGSQGLKHIAKRVHNATLILSEGLKRAGHQLQHDL-FFDTLKVQCGCSVKEVLGRAAQRQI- 463
Cdd:PRK00451 327 ICTNQALNALAAAIYMSLLGPEGLRELAEQNHQKAHYLAERLAEIGGVELFDGpFFNEFVVRLPKPAEEVNEALLEKGIl 406
|
410 420 430
....*....|....*....|....*....|...
gi 20070408 464 -------NFRLFDDGTLgISLDETVTEKDLDDL 489
Cdd:PRK00451 407 ggydlgrYYPELGNHLL-VCVTEKRTKEDIDAL 438
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
603-762 |
1.53e-10 |
|
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: 60.86 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 603 LEKDLCEIT--GYDRVSFQPnSGAQGEYAGLATIRayldqkgERHRTVcLIPKSAHGTNPAS-AHMAGMKIQPVEVDRYG 679
Cdd:cd01494 5 LEEKLARLLqpGNDKAVFVP-SGTGANEAALLALL-------GPGDEV-IVDANGHGSRYWVaAELAGAKPVPVPVDDAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 680 NiDVAHLKAMVD-QHKENLAAIMITYPSTNGVFEENIGDVCALIHQHGGQVYLDGANMNAQVGI--CRPGDFGSDVSHLN 756
Cdd:cd01494 76 Y-GGLDVAILEElKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPApgVLIPEGGADVVTFS 154
|
....*.
gi 20070408 757 LHKTFC 762
Cdd:cd01494 155 LHKNLG 160
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
591-734 |
2.67e-06 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 50.29 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 591 DQAQGYQQLFQGLEKDLCEITGYDRVSFQPnSGAQGEYAGLATirayLDQKGerHRTVCLIPksAHG---TNPASAHMAG 667
Cdd:pfam01212 25 DEVYGGDPTVNRLEDRVAELFGKEAALFVP-SGTAANQLALMA----HCQRG--DEVICGEP--AHIhfdETGGHAELGG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20070408 668 MKIQPVEVDRYGNIDVAHLKAMVDQHK----ENLAAIMITypSTNG------VFEENIGDVCALIHQHGGQVYLDGA 734
Cdd:pfam01212 96 VQPRPLDGDEAGNMDLEDLEAAIREVGadifPPTGLISLE--NTHNsaggqvVSLENLREIAALAREHGIPVHLDGA 170
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
822-928 |
2.58e-05 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 47.83 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 822 YIKMMGGKGLKEATEIAILNANYMAKRLEKH-YRVLFRGARGyvaHEFILDTrpfkksaNVEAVDVAKRLQDYGFHA--- 897
Cdd:PRK00451 341 YMSLLGPEGLRELAEQNHQKAHYLAERLAEIgGVELFDGPFF---NEFVVRL-------PKPAEEVNEALLEKGILGgyd 410
|
90 100 110
....*....|....*....|....*....|....*.
gi 20070408 898 -----PTMswpvAGTLMIEPTESEDKAELDRFCDAM 928
Cdd:PRK00451 411 lgryyPEL----GNHLLVCVTEKRTKEDIDALVAAL 442
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
663-752 |
2.56e-04 |
|
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: 44.64 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 663 AHMAGMKIqpVEVDRY-GNIDVAHLKAMVDqhkENLAAIMITYPSTNGVFEEnIGDVCALIHQHGGQVYLdGANMNAQVG 741
Cdd:COG0403 176 AEPLGIEV--VEVPDEdGVTDLEALKALLD---DDVAGVLVQYPNFFGVIED-LRAIAEAAHAAGALVIV-AADPLSLGL 248
|
90
....*....|.
gi 20070408 742 ICRPGDFGSDV 752
Cdd:COG0403 249 LKPPGELGADI 259
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
826-928 |
3.37e-04 |
|
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: 44.25 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 826 MGGKGLKEATEIAILNANYMAKRLEK-HYRVLFRGArgyVAHEFILDTrpfkksaNVEAVDVAKRLQDYGFHAPT-MSWP 903
Cdd:COG0403 346 HGPEGLKEIAERIHQKAHYLAERLAAlGVEVPFNGP---FFDEFVVRL-------PKPAAEINAALLEKGILGGLnLRRV 415
|
90 100
....*....|....*....|....*
gi 20070408 904 VAGTLMIEPTESEDKAELDRFCDAM 928
Cdd:COG0403 416 DDDTLLVAVTETTTKEDIDALVEAL 440
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
628-734 |
7.65e-04 |
|
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: 42.96 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070408 628 YAGLAT---IRAYLDQKGER--HRTVCLIPKSAHGTNPASAHMAGMKIQPVEVDRYGNIDVAHLKAMVDQHK-ENLAAIM 701
Cdd:cd06450 72 LALLAArdrARKRLKAGGGRgiDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKaEGLNPIM 151
|
90 100 110
....*....|....*....|....*....|....*...
gi 20070408 702 I--TYPSTN-GVFE--ENIGDVCaliHQHGGQVYLDGA 734
Cdd:cd06450 152 VvaTAGTTDtGAIDplEEIADLA---EKYDLWLHVDAA 186
|
|
| tnaA |
PRK13238 |
tryptophanase; |
679-734 |
4.31e-03 |
|
tryptophanase;
Pssm-ID: 237314 Cd Length: 460 Bit Score: 40.95 E-value: 4.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20070408 679 GNIDVAHLKAMVDQH-KENLAAIMITypSTNG------VFEENIGDVCALIHQHGGQVYLDGA 734
Cdd:PRK13238 159 GNFDLEKLEALIEEVgAENVPFIVMT--ITNNsaggqpVSMANLRAVYEIAKKYGIPVVIDAA 219
|
|
|