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Conserved domains on  [gi|1222443639|ref|WP_090495053|]
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cysteine desulfurase-like protein [Pseudoalteromonas sp. DSM 26666]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 6-403 2.84e-175

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).


The actual alignment was detected with superfamily member TIGR01976:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 397  Bit Score: 494.66  E-value: 2.84e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   6 LRAQFPALMQTVDgkspVFLDGPGGSQVPQSVLSAMTAYLGHYNSNLGGAFFSSDKTVELMANARQAAADLLNApSAQNI 85
Cdd:TIGR01976   6 VRGQFPALADGDR----VFFDNPAGTQIPQSVADAVSAALTRSNANRGGAYESSRRADQVVDDAREAVADLLNA-DPPEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  86 VFGPNMTSLTFSFSRAISRNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEADCSLDMAHFESLLNSNTKLV 165
Cdd:TIGR01976  81 VFGANATSLTFLLSRAISRRWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEATGELHPDDLASLLSPRTRLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 166 AVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPHLGMVYGKTEHLEGFTPY 245
Cdd:TIGR01976 161 AVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPHMGILWGRPELLMNLPPY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 246 KVEPAKDVAPGRWETGTQSFEALAGFIAAVDYIAAISElDDSHSRREKLRVAFAKTKQHEMALSEYFLTRLVNYPKIKLF 325
Cdd:TIGR01976 241 KLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGE-SANGSRRERLVASFQAIDAYENRLAEYLLVGLSDLPGVTLY 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222443639 326 GIddlERLSERTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFYAQGLCKQLGVLDKGGVVRIGCMHYNTLEEMDTLF 403
Cdd:TIGR01976 320 GV---ARLAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNDEGGVVRVGLAHYNTAEEVDRLL 394
 
Name Accession Description Interval E-value
am_tr_V_VC1184 TIGR01976
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ...
 6-403 2.84e-175

cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273906 [Multi-domain]  Cd Length: 397  Bit Score: 494.66  E-value: 2.84e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   6 LRAQFPALMQTVDgkspVFLDGPGGSQVPQSVLSAMTAYLGHYNSNLGGAFFSSDKTVELMANARQAAADLLNApSAQNI 85
Cdd:TIGR01976   6 VRGQFPALADGDR----VFFDNPAGTQIPQSVADAVSAALTRSNANRGGAYESSRRADQVVDDAREAVADLLNA-DPPEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  86 VFGPNMTSLTFSFSRAISRNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEADCSLDMAHFESLLNSNTKLV 165
Cdd:TIGR01976  81 VFGANATSLTFLLSRAISRRWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEATGELHPDDLASLLSPRTRLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 166 AVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPHLGMVYGKTEHLEGFTPY 245
Cdd:TIGR01976 161 AVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPHMGILWGRPELLMNLPPY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 246 KVEPAKDVAPGRWETGTQSFEALAGFIAAVDYIAAISElDDSHSRREKLRVAFAKTKQHEMALSEYFLTRLVNYPKIKLF 325
Cdd:TIGR01976 241 KLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGE-SANGSRRERLVASFQAIDAYENRLAEYLLVGLSDLPGVTLY 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222443639 326 GIddlERLSERTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFYAQGLCKQLGVLDKGGVVRIGCMHYNTLEEMDTLF 403
Cdd:TIGR01976 320 GV---ARLAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNDEGGVVRVGLAHYNTAEEVDRLL 394
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
2-410 5.63e-108

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 323.24  E-value: 5.63e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   2 NLMQLRAQFPALmqtvdGKSPVFLDGPGGSQVPQSVLSAMTAYLGHYNSNLG-GAFFSSDKTVELMANARQAAADLLNAP 80
Cdd:COG0520     1 DVEAIRADFPVL-----GKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  81 SAQNIVFGPNMTSLTFSFSRAISRnWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAHFESLLNS 160
Cdd:COG0520    76 SPDEIIFTRGTTEAINLVAYGLGR-LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDE-DGELDLEALEALLTP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 161 NTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMVYGKTEHL 239
Cdd:COG0520   154 RTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTgIGVLYGKRELL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 240 EGFTPYKV--EPAKDV---------APGRWETGTQSFEALAGFIAAVDYIAAIselddshsrreklrvAFAKTKQHEMAL 308
Cdd:COG0520   234 EALPPFLGggGMIEWVsfdgttyadLPRRFEAGTPNIAGAIGLGAAIDYLEAI---------------GMEAIEAREREL 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 309 SEYFLTRLVNYPKIKLFGIDDLErlsERTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFYAQGLCKQLGVldkGGVVRI 388
Cdd:COG0520   299 TAYALEGLAAIPGVRILGPADPE---DRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGV---PGTVRA 372

                         410       420
                  ....*....|....*....|..
gi 1222443639 389 GCMHYNTLEEMDTLFNLFDELI 410
Cdd:COG0520   373 SFHLYNTEEEIDRLVEALKKLA 394
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 23-402 2.55e-87

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 269.72  E-value: 2.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  23 VFLDGPGGSQVPQSVLSAMTAYLGHYNSNLG-GAFFSSDKTVELMANARQAAADLLNAPSAQNIVFGPNMTS----LTFS 97
Cdd:cd06453     1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEainlVAYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  98 FSRAIsrnwQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAHFESLLNSNTKLVAVTYASNTTGSI 177
Cdd:cd06453    81 LGRAN----KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDD-DGQLDLEALEKLLTERTKLVAVTHVSNVLGTI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 178 NDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMVYGKTEHLEGFTPYKV--EPAKDVA 254
Cdd:cd06453   156 NPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTgIGVLYGKEELLEEMPPYGGggEMIEEVS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 255 ---------PGRWETGTQSFEALAGFIAAVDYIAAISelddshsrREKLRvafaktkQHEMALSEYFLTRLVNYPKIKLF 325
Cdd:cd06453   236 feettyadlPHKFEAGTPNIAGAIGLGAAIDYLEKIG--------MEAIA-------AHEHELTAYALERLSEIPGVRVY 300

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222443639 326 GiddleRLSERTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFYAQGLCKQLGVldkGGVVRIGCMHYNTLEEMDTL 402
Cdd:cd06453   301 G-----DAEDRAGVVSFNLEGIHPHDVATILDQYGIAVRAGHHCAQPLMRRLGV---PGTVRASFGLYNTEEEIDAL 369
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 23-402 5.12e-82

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 256.02  E-value: 5.12e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  23 VFLDGPGGSQVPQSVLSAMTAYLGHYNSNLGGAFFS-SDKTVELMANARQAAADLLNAPSAQNIVFGPNMTSLTFSFSRA 101
Cdd:pfam00266   1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTlGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 102 ISRNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAHFESLLNSNTKLVAVTYASNTTGSINDIK 181
Cdd:pfam00266  81 LGRSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDE-DGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 182 RIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMVYGKTEHLEGFTPYKV--EPAKDV----- 253
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTgIGVLYGRRDLLEKMPPLLGggGMIETVslqes 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 254 ----APGRWETGTQSFEALAGFIAAVDYIAAISelddshsrreklrvaFAKTKQHEMALSEYFLTRLVNYPKIKLFGIDd 329
Cdd:pfam00266 240 tfadAPWKFEAGTPNIAGIIGLGAALEYLSEIG---------------LEAIEKHEHELAQYLYERLLSLPGIRLYGPE- 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222443639 330 lerlsERTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFYAQGLCKQLGVldkGGVVRIGCMHYNTLEEMDTL 402
Cdd:pfam00266 304 -----RRASIISFNFKGVHPHDVATLLDESGIAVRSGHHCAQPLMVRLGL---GGTVRASFYIYNTQEDVDRL 368
PLN02855 PLN02855
Bifunctional selenocysteine lyase/cysteine desulfurase
 6-402 7.28e-79

Bifunctional selenocysteine lyase/cysteine desulfurase


Pssm-ID: 215460 [Multi-domain]  Cd Length: 424  Bit Score: 249.66  E-value: 7.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   6 LRAQFPALMQTVDGKSPVFLDGPGGSQVPQSVLSAMTAYLGHYNSNLG-GAFFSSDKTVELMANARQAAADLLNAPSAQN 84
Cdd:PLN02855   17 TRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHrGIHALSAKATDAYELARKKVAAFINASTSRE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  85 IVFGPNMTS----LTFSFSRAisrNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAHFESLLNS 160
Cdd:PLN02855   97 IVFTRNATEainlVAYTWGLA---NLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTP-DEVLDVEQLKELLSE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 161 NTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMVYGKTEHL 239
Cdd:PLN02855  173 KTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTgIGFLWGKSDLL 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 240 EGFTPYK--VEPAKDV---------APGRWETGTQSFEALAGFIAAVDYIAAISeLDDSHSrreklrvafaktkqHEMAL 308
Cdd:PLN02855  253 ESMPPFLggGEMISDVfldhstyapPPSRFEAGTPAIGEAIGLGAAIDYLSEIG-MDRIHE--------------YEVEL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 309 SEYFLTRLVNYPKIKLFGIDDLERlSERTPTFALTFEGLEPRQVSEFLGKQH-VCVWDGNFYAQGLCKQLGVldkGGVVR 387
Cdd:PLN02855  318 GTYLYEKLSSVPGVRIYGPKPSEG-VGRAALCAFNVEGIHPTDLSTFLDQQHgVAIRSGHHCAQPLHRYLGV---NASAR 393

                         410
                  ....*....|....*
gi 1222443639 388 IGCMHYNTLEEMDTL 402
Cdd:PLN02855  394 ASLYFYNTKEEVDAF 408
f2_encap_cargo1 NF041166
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ...
 7-281 4.94e-48

family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.


Pssm-ID: 469077 [Multi-domain]  Cd Length: 623  Bit Score: 172.73  E-value: 4.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   7 RAQFPALMQTVDGKSPVFLDGPGGSQVPQSVLSAMTAYLGHYNSNLGGAffssdkTVELMA-------NARQAAADLLNA 79
Cdd:NF041166  231 RRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRA------AHELAAratdayeGAREKVRRFIGA 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  80 PSAQNIVF------GPNMTSLTFSfsraiSRNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAH 153
Cdd:NF041166  305 PSVDEIIFvrgtteAINLVAKSWG-----RQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDD-SGQILLDE 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 154 FESLLNSNTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMV 232
Cdd:NF041166  379 YAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTgIGVV 458

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222443639 233 YGKTEHLEGFTPYK--------VEPAKDV---APGRWETGTqsfealaGFIA-------AVDYIAAI 281
Cdd:NF041166  459 YGKRDLLEAMPPWQgggnmiadVTFEKTVyqpAPNRFEAGT-------GNIAdavglgaALDYVERI 518
 
Name Accession Description Interval E-value
am_tr_V_VC1184 TIGR01976
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ...
 6-403 2.84e-175

cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273906 [Multi-domain]  Cd Length: 397  Bit Score: 494.66  E-value: 2.84e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   6 LRAQFPALMQTVDgkspVFLDGPGGSQVPQSVLSAMTAYLGHYNSNLGGAFFSSDKTVELMANARQAAADLLNApSAQNI 85
Cdd:TIGR01976   6 VRGQFPALADGDR----VFFDNPAGTQIPQSVADAVSAALTRSNANRGGAYESSRRADQVVDDAREAVADLLNA-DPPEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  86 VFGPNMTSLTFSFSRAISRNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEADCSLDMAHFESLLNSNTKLV 165
Cdd:TIGR01976  81 VFGANATSLTFLLSRAISRRWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEATGELHPDDLASLLSPRTRLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 166 AVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPHLGMVYGKTEHLEGFTPY 245
Cdd:TIGR01976 161 AVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPHMGILWGRPELLMNLPPY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 246 KVEPAKDVAPGRWETGTQSFEALAGFIAAVDYIAAISElDDSHSRREKLRVAFAKTKQHEMALSEYFLTRLVNYPKIKLF 325
Cdd:TIGR01976 241 KLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGE-SANGSRRERLVASFQAIDAYENRLAEYLLVGLSDLPGVTLY 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222443639 326 GIddlERLSERTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFYAQGLCKQLGVLDKGGVVRIGCMHYNTLEEMDTLF 403
Cdd:TIGR01976 320 GV---ARLAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNDEGGVVRVGLAHYNTAEEVDRLL 394
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
2-410 5.63e-108

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 323.24  E-value: 5.63e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   2 NLMQLRAQFPALmqtvdGKSPVFLDGPGGSQVPQSVLSAMTAYLGHYNSNLG-GAFFSSDKTVELMANARQAAADLLNAP 80
Cdd:COG0520     1 DVEAIRADFPVL-----GKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  81 SAQNIVFGPNMTSLTFSFSRAISRnWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAHFESLLNS 160
Cdd:COG0520    76 SPDEIIFTRGTTEAINLVAYGLGR-LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDE-DGELDLEALEALLTP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 161 NTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMVYGKTEHL 239
Cdd:COG0520   154 RTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTgIGVLYGKRELL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 240 EGFTPYKV--EPAKDV---------APGRWETGTQSFEALAGFIAAVDYIAAIselddshsrreklrvAFAKTKQHEMAL 308
Cdd:COG0520   234 EALPPFLGggGMIEWVsfdgttyadLPRRFEAGTPNIAGAIGLGAAIDYLEAI---------------GMEAIEAREREL 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 309 SEYFLTRLVNYPKIKLFGIDDLErlsERTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFYAQGLCKQLGVldkGGVVRI 388
Cdd:COG0520   299 TAYALEGLAAIPGVRILGPADPE---DRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGV---PGTVRA 372

                         410       420
                  ....*....|....*....|..
gi 1222443639 389 GCMHYNTLEEMDTLFNLFDELI 410
Cdd:COG0520   373 SFHLYNTEEEIDRLVEALKKLA 394
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 23-402 2.55e-87

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 269.72  E-value: 2.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  23 VFLDGPGGSQVPQSVLSAMTAYLGHYNSNLG-GAFFSSDKTVELMANARQAAADLLNAPSAQNIVFGPNMTS----LTFS 97
Cdd:cd06453     1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEainlVAYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  98 FSRAIsrnwQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAHFESLLNSNTKLVAVTYASNTTGSI 177
Cdd:cd06453    81 LGRAN----KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDD-DGQLDLEALEKLLTERTKLVAVTHVSNVLGTI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 178 NDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMVYGKTEHLEGFTPYKV--EPAKDVA 254
Cdd:cd06453   156 NPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTgIGVLYGKEELLEEMPPYGGggEMIEEVS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 255 ---------PGRWETGTQSFEALAGFIAAVDYIAAISelddshsrREKLRvafaktkQHEMALSEYFLTRLVNYPKIKLF 325
Cdd:cd06453   236 feettyadlPHKFEAGTPNIAGAIGLGAAIDYLEKIG--------MEAIA-------AHEHELTAYALERLSEIPGVRVY 300

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222443639 326 GiddleRLSERTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFYAQGLCKQLGVldkGGVVRIGCMHYNTLEEMDTL 402
Cdd:cd06453   301 G-----DAEDRAGVVSFNLEGIHPHDVATILDQYGIAVRAGHHCAQPLMRRLGV---PGTVRASFGLYNTEEEIDAL 369
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 23-402 5.12e-82

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 256.02  E-value: 5.12e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  23 VFLDGPGGSQVPQSVLSAMTAYLGHYNSNLGGAFFS-SDKTVELMANARQAAADLLNAPSAQNIVFGPNMTSLTFSFSRA 101
Cdd:pfam00266   1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTlGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 102 ISRNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAHFESLLNSNTKLVAVTYASNTTGSINDIK 181
Cdd:pfam00266  81 LGRSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDE-DGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 182 RIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMVYGKTEHLEGFTPYKV--EPAKDV----- 253
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTgIGVLYGRRDLLEKMPPLLGggGMIETVslqes 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 254 ----APGRWETGTQSFEALAGFIAAVDYIAAISelddshsrreklrvaFAKTKQHEMALSEYFLTRLVNYPKIKLFGIDd 329
Cdd:pfam00266 240 tfadAPWKFEAGTPNIAGIIGLGAALEYLSEIG---------------LEAIEKHEHELAQYLYERLLSLPGIRLYGPE- 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222443639 330 lerlsERTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFYAQGLCKQLGVldkGGVVRIGCMHYNTLEEMDTL 402
Cdd:pfam00266 304 -----RRASIISFNFKGVHPHDVATLLDESGIAVRSGHHCAQPLMVRLGL---GGTVRASFYIYNTQEDVDRL 368
PLN02855 PLN02855
Bifunctional selenocysteine lyase/cysteine desulfurase
 6-402 7.28e-79

Bifunctional selenocysteine lyase/cysteine desulfurase


Pssm-ID: 215460 [Multi-domain]  Cd Length: 424  Bit Score: 249.66  E-value: 7.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   6 LRAQFPALMQTVDGKSPVFLDGPGGSQVPQSVLSAMTAYLGHYNSNLG-GAFFSSDKTVELMANARQAAADLLNAPSAQN 84
Cdd:PLN02855   17 TRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHrGIHALSAKATDAYELARKKVAAFINASTSRE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  85 IVFGPNMTS----LTFSFSRAisrNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAHFESLLNS 160
Cdd:PLN02855   97 IVFTRNATEainlVAYTWGLA---NLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTP-DEVLDVEQLKELLSE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 161 NTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMVYGKTEHL 239
Cdd:PLN02855  173 KTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTgIGFLWGKSDLL 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 240 EGFTPYK--VEPAKDV---------APGRWETGTQSFEALAGFIAAVDYIAAISeLDDSHSrreklrvafaktkqHEMAL 308
Cdd:PLN02855  253 ESMPPFLggGEMISDVfldhstyapPPSRFEAGTPAIGEAIGLGAAIDYLSEIG-MDRIHE--------------YEVEL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 309 SEYFLTRLVNYPKIKLFGIDDLERlSERTPTFALTFEGLEPRQVSEFLGKQH-VCVWDGNFYAQGLCKQLGVldkGGVVR 387
Cdd:PLN02855  318 GTYLYEKLSSVPGVRIYGPKPSEG-VGRAALCAFNVEGIHPTDLSTFLDQQHgVAIRSGHHCAQPLHRYLGV---NASAR 393

                         410
                  ....*....|....*
gi 1222443639 388 IGCMHYNTLEEMDTL 402
Cdd:PLN02855  394 ASLYFYNTKEEVDAF 408
PRK09295 PRK09295
cysteine desulfurase SufS;
5-402 1.80e-55

cysteine desulfurase SufS;


Pssm-ID: 181766 [Multi-domain]  Cd Length: 406  Bit Score: 188.42  E-value: 1.80e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   5 QLRAQFPALMQTVDGKSPVFLDGPGGSQVPQSVLSAMTAYLGH-YNSNLGGAFFSSDKTVELMANARQAAADLLNAPSAQ 83
Cdd:PRK09295    7 KVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHgYAAVHRGIHTLSAQATEKMENVRKQAALFINARSAE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  84 NIVF------GPNMTSLTFSfsraiSRNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAHFESL 157
Cdd:PRK09295   87 ELVFvrgtteGINLVANSWG-----NSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNP-DGTLQLETLPAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 158 LNSNTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMVYGKT 236
Cdd:PRK09295  161 FDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTgIGILYVKE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 237 EHLEGFTPYK--------VEPAKDV----APGRWETGTQSFEALAGFIAAVDYIAAIselddshsrreklrvAFAKTKQH 304
Cdd:PRK09295  241 ALLQEMPPWEgggsmiatVSLTEGTtwakAPWRFEAGTPNTGGIIGLGAALDYVSAL---------------GLNNIAEY 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 305 EMALSEYFLTRLVNYPKIKLFGIDdlerlsERTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFYAQGLCKQLGVldkGG 384
Cdd:PRK09295  306 EQNLMHYALSQLESVPDLTLYGPQ------NRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNV---PA 376

                         410
                  ....*....|....*...
gi 1222443639 385 VVRIGCMHYNTLEEMDTL 402
Cdd:PRK09295  377 MCRASLAMYNTHEEVDRL 394
PRK10874 PRK10874
cysteine desulfurase CsdA;
2-402 2.06e-54

cysteine desulfurase CsdA;


Pssm-ID: 182799 [Multi-domain]  Cd Length: 401  Bit Score: 185.24  E-value: 2.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   2 NLMQLRAQFPALMQtvdgkSPVFLDGPGGSQVPQSVLSAMTAYlghYNSNLG----GAFFSSDKTVELMANARQAAADLL 77
Cdd:PRK10874    5 NPAQFRAQFPALQD-----AGVYLDSAATALKPQAVIEATQQF---YSLSAGnvhrSQFAAAQRLTARYEAAREQVAQLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  78 NAPSAQNIVFGPNMT-SLTF---SFSRAisrNWQAGDEIIVTNADHFSNVSSWQQAAEDKGV-VVNTALvnEADCSLDMA 152
Cdd:PRK10874   77 NAPDAKNIVWTRGTTeSINLvaqSYARP---RLQPGDEIIVSEAEHHANLVPWLMVAQQTGAkVVKLPL--GADRLPDVD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 153 HFESLLNSNTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVD----AVHYAPheliDVQALDCDFLACSAYKFFGPH 228
Cdd:PRK10874  152 LLPELITPRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDgaqgAVHFPA----DVQALDIDFYAFSGHKLYGPT 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 229 -LGMVYGKTEHLE------------------GFTPYKVepakdvaPGRWETGTQSFEALAGFIAAVDYIAAISelddshs 289
Cdd:PRK10874  228 gIGVLYGKSELLEamspwqgggkmltevsfdGFTPQSA-------PWRFEAGTPNVAGVIGLSAALEWLADID------- 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 290 rreklrvaFAKTKQHEMALSEYFLTRLVNYPKIKLFGIDDlerlserTPTFALTFEGLEPRQVSEFLGKQHVCVWDGNFY 369
Cdd:PRK10874  294 --------INQAESWSRSLATLAEDALAKLPGFRSFRCQD-------SSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHC 358

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1222443639 370 AQGLCKQLGVldkGGVVRIGCMHYNTLEEMDTL 402
Cdd:PRK10874  359 AQPLLAALGV---TGTLRASFAPYNTQSDVDAL 388
f2_encap_cargo1 NF041166
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ...
 7-281 4.94e-48

family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.


Pssm-ID: 469077 [Multi-domain]  Cd Length: 623  Bit Score: 172.73  E-value: 4.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639   7 RAQFPALMQTVDGKSPVFLDGPGGSQVPQSVLSAMTAYLGHYNSNLGGAffssdkTVELMA-------NARQAAADLLNA 79
Cdd:NF041166  231 RRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRA------AHELAAratdayeGAREKVRRFIGA 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  80 PSAQNIVF------GPNMTSLTFSfsraiSRNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEaDCSLDMAH 153
Cdd:NF041166  305 PSVDEIIFvrgtteAINLVAKSWG-----RQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDD-SGQILLDE 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 154 FESLLNSNTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMV 232
Cdd:NF041166  379 YAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTgIGVV 458

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222443639 233 YGKTEHLEGFTPYK--------VEPAKDV---APGRWETGTqsfealaGFIA-------AVDYIAAI 281
Cdd:NF041166  459 YGKRDLLEAMPPWQgggnmiadVTFEKTVyqpAPNRFEAGT-------GNIAdavglgaALDYVERI 518
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 37-363 4.26e-30

Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];


Pssm-ID: 440721 [Multi-domain]  Cd Length: 381  Bit Score: 119.38  E-value: 4.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  37 VLSAMTAYLGHYNSN------LGGAffsSDKTVElmaNARQAAADLLNApSAQNIVFgpnmTS-------LtfsfsrAI- 102
Cdd:COG1104    18 VLEAMLPYLTEYFGNpsslhsFGRE---ARAALE---EAREQVAALLGA-DPEEIIF----TSggteannL------AIk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 103 ---SRNWQAGDEIIVTNADHFSnVSSWQQAAEDKGVVVnTAL-VNEaDCSLDMAHFESLLNSNTKLVAVTYASNTTGSIN 178
Cdd:COG1104    81 gaaRAYRKKGKHIITSAIEHPA-VLETARFLEKEGFEV-TYLpVDE-DGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 179 DIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGPH-LGMVYGKTEHlegftpyKVEPakdVAPG- 256
Cdd:COG1104   158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKgVGALYVRKGV-------RLEP---LIHGg 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 257 ----RWETGTQSFEALAGFIAAVDyiAAISELDDSHSRREKLRvafaktkqhemalsEYFLTRLV-NYPKIKLFGiddle 331
Cdd:COG1104   228 gqerGLRSGTENVPGIVGLGKAAE--LAAEELEEEAARLRALR--------------DRLEEGLLaAIPGVVING----- 286

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1222443639 332 RLSERTP-TFALTFEGLEPRQVSEFLGKQHVCV 363
Cdd:COG1104   287 DPENRLPnTLNFSFPGVEGEALLLALDLAGIAV 319
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
40-298 2.74e-16

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 79.77  E-value: 2.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  40 AMTAYLGHYNS--NLGGaffssdKTVELMANARQAAADLLNApSAQNIVFGPNMTSLTF----SFSRAISRNwqaGDEII 113
Cdd:PRK02948   23 AASQYFGNESSlhDIGG------TASSLLQVCRKTFAEMIGG-EEQGIYFTSGGTESNYlaiqSLLNALPQN---KKHII 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 114 VTNADHFSnVSSWQQAAEDKGVVVNTALVNEADcSLDMAHFESLLNSNTKLVAVTYASNTTGSINDIKRIIELAHNVGAL 193
Cdd:PRK02948   93 TTPMEHAS-IHSYFQSLESQGYTVTEIPVDKSG-LIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEIGALLKKYNVL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 194 VYVDAVHYAPHELIDVQALDCDFLACSAYKFFGP------------HLGMVYGKTEHLEGFTPykvepakdvapgrwetG 261
Cdd:PRK02948  171 FHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPkgvgavyinpqvRWKPVFPGTTHEKGFRP----------------G 234

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1222443639 262 TQSFEALAGFIAAVDYIaaISELDDSHSRREKLRVAF 298
Cdd:PRK02948  235 TVNVPGIAAFLTAAENI--LKNMQEESLRFKELRSYF 269
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
20-227 4.38e-15

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 76.52  E-value: 4.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  20 KSPVFLDGPGGSQVPQSVLSAMTAYLG--------HYNSNLGGafFSSDKTVElmaNARQAAADLLNApSAQNIVFgpnm 91
Cdd:PRK14012    2 KLPIYLDYSATTPVDPRVAEKMMPYLTmdgtfgnpASRSHRFG--WQAEEAVD---IARNQIADLIGA-DPREIVF---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  92 TS-LTFSFSRAI---SRNWQA-GDEIIVTNADHFSNVSSWQQAaEDKGVVVnTALVNEADCSLDMAHFESLLNSNTKLVA 166
Cdd:PRK14012   72 TSgATESDNLAIkgaAHFYQKkGKHIITSKTEHKAVLDTCRQL-EREGFEV-TYLDPQSNGIIDLEKLEAAMRDDTILVS 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222443639 167 VTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGP 227
Cdd:PRK14012  150 IMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGP 210
PLN02651 PLN02651
cysteine desulfurase
 23-227 9.06e-11

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 62.75  E-value: 9.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  23 VFLDGPGGSQVPQSVLSAMTAYL-GHYN--SNLGGAF-FSSDKTVElmaNARQAAADLLNAPSAQnIVFGPNMT-SLTFS 97
Cdd:PLN02651    1 LYLDMQATTPIDPRVLDAMLPFLiEHFGnpHSRTHLYgWESEDAVE---KARAQVAALIGADPKE-IIFTSGATeSNNLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  98 FSRAISRNWQAGDEIIVTNADHfSNVSSWQQAAEDKGVVVnTALVNEADCSLDMAHFESLLNSNTKLVAVTYASNTTGSI 177
Cdd:PLN02651   77 IKGVMHFYKDKKKHVITTQTEH-KCVLDSCRHLQQEGFEV-TYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1222443639 178 NDIKRIIELAHNVGALVYVDAVHYAPHELIDVQALDCDFLACSAYKFFGP 227
Cdd:PLN02651  155 QPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGP 204
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 24-199 4.28e-09

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 57.69  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  24 FLDGPGGSQVPQSVLSAMTaylghyNSNLGgafFSSDKTVELMANARQAAADLLNAPSAQNIVFGpnmTSLTFSFSRAIS 103
Cdd:cd06451     1 LLLIPGPSNVPPRVLKAMN------RPMLG---HRSPEFLALMDEILEGLRYVFQTENGLTFLLS---GSGTGAMEAALS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 104 RNWQAGDEIIVTNADHFSNvsSWQQAAEDKG--VVVNTALVNEAdcsLDMAHFESLLNSNT-KLVAVTYASNTTGSINDI 180
Cdd:cd06451    69 NLLEPGDKVLVGVNGVFGD--RWADMAERYGadVDVVEKPWGEA---VSPEEIAEALEQHDiKAVTLTHNETSTGVLNPL 143

                         170
                  ....*....|....*....
gi 1222443639 181 KRIIELAHNVGALVYVDAV 199
Cdd:cd06451   144 EGIGALAKKHDALLIVDAV 162
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 27-199 2.55e-08

Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 55.48  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  27 GPGGSQVPQSVLSAM-TAYLGHYnsnlGGAFfssdktVELMANARQAAADLLNApsaQNIVF---GPNMTSLTFSFSRAI 102
Cdd:COG0075     5 TPGPTPVPPRVLRAMaRPMIGHR----DPEF------VELMDEVRELLKKVFGT---ENDVViltGSGTGAMEAALANLV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 103 SRnwqaGDEIIVTNADHFSNvsSWQQAAEDKGVVVnTALVNEADCSLDMAHFESLLNSNT--KLVAVTYASNTTGSINDI 180
Cdd:COG0075    72 SP----GDKVLVLVNGAFGE--RWAEIAERYGAEV-VVLEVPWGEAVDPEEVEEALAADPdiKAVAVVHNETSTGVLNPL 144

                         170
                  ....*....|....*....
gi 1222443639 181 KRIIELAHNVGALVYVDAV 199
Cdd:COG0075   145 EEIGALAKEHGALLIVDAV 163
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 70-213 7.77e-08

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: 53.88  E-value: 7.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  70 RQAAADLLN-----APSAQNIVFGPNMTSLTFSFSRAISRnwqAGDEIIVTNADHFSNVSSWQQAaedKGVVVNTALVNE 144
Cdd:cd00609    42 REAIAEWLGrrggvDVPPEEIVVTNGAQEALSLLLRALLN---PGDEVLVPDPTYPGYEAAARLA---GAEVVPVPLDEE 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443639 145 ADCSLDMAHFESLLNSNTKLVAVTYASNTTGSI---NDIKRIIELAHNVGALVYVDAVH----YAPHELIDVQALD 213
Cdd:cd00609   116 GGFLLDLELLEAAKTPKTKLLYLNNPNNPTGAVlseEELEELAELAKKHGILIISDEAYaelvYDGEPPPALALLD 191
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
70-200 1.42e-07

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 53.08  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  70 RQAAADLLNAP------SAQNIVFGPNMTSLTFSFSRAISrnwQAGDEIIVTNADHfsnvSSWQQAAED-KGVVVNTALV 142
Cdd:pfam00155  45 REALAKFLGRSpvlkldREAAVVFGSGAGANIEALIFLLA---NPGDAILVPAPTY----ASYIRIARLaGGEVVRYPLY 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222443639 143 NEADCSLDMAHFESLLNSNTKLVAVTYASNTTGSI---NDIKRIIELAHNVGALVYVDAVH 200
Cdd:pfam00155 118 DSNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVatlEELEKLLDLAKEHNILLLVDEAY 178
Cys_Met_Meta_PP pfam01053
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ...
 107-228 3.08e-07

Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.


Pssm-ID: 395837 [Multi-domain]  Cd Length: 376  Bit Score: 51.85  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 107 QAGDEIIVTNA------DHFSNVSSWQQAaedKGVVVNTALVNEadcsldmahFESLLNSNTKLVAVTYASNTTGSINDI 180
Cdd:pfam01053  84 KAGDHIVATDDlyggtyRLFNKVLPRFGI---EVTFVDTSDPED---------LEAAIKPNTKAVYLETPTNPLLKVVDI 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1222443639 181 KRIIELAHNVGALVYVDAVHYAPHeLIDVQALDCDFLACSAYKFFGPH 228
Cdd:pfam01053 152 EAIAKLAKKHGILVVVDNTFASPY-LQRPLDLGADIVVHSATKYIGGH 198
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 101-254 6.73e-07

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: 51.08  E-value: 6.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 101 AISRNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVVNTALVNEADCsLDMAHFESLLNSNTKLVAVTYAsNTTGSI-ND 179
Cdd:cd00613   100 AAIRAYHKRNKVLVPDSAHPTNPAVARTRGEPLGIEVVEVPSDEGGT-VDLEALKEEVSEEVAALMVQYP-NTLGVFeDL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 180 IKRIIELAHNVGALVYVDAvhyAPHELI------DVQAldcDFLACSAYKFF------GPHLGMVyGKTEHLEGFTPYK- 246
Cdd:cd00613   178 IKEIADIAHSAGALVYVDG---DNLNLTglkppgEYGA---DIVVGNLQKTGvphgggGPGAGFF-AVKKELVRFLPGRl 250


                  ....*...
gi 1222443639 247 VEPAKDVA 254
Cdd:cd00613   251 VGVTKDAE 258
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 65-235 1.30e-06

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: 48.15  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  65 LMANARQAAADLLNaPSAQNIVF-----GPNMTSLTFSFsraisrnwQAGDEIIVTNADHFSNVSSwqqAAEDKGVVVNT 139
Cdd:cd01494     1 KLEELEEKLARLLQ-PGNDKAVFvpsgtGANEAALLALL--------GPGDEVIVDANGHGSRYWV---AAELAGAKPVP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 140 ALVNEA-DCSLDMAHFESLLNS-NTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVH-----YAPHELIDVQal 212
Cdd:cd01494    69 VPVDDAgYGGLDVAILEELKAKpNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASaggasPAPGVLIPEG-- 146

                         170       180
                  ....*....|....*....|....
gi 1222443639 213 DCDFLACSAYKFF-GPHLGMVYGK 235
Cdd:cd01494   147 GADVVTFSLHKNLgGEGGGVVIVK 170
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 149-306 7.90e-06

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: 47.56  E-value: 7.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 149 LDMAHFESLLNSNT-----KLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHyaphelidvqaldcdflacsAYK 223
Cdd:cd06454   115 NDMEDLEKLLREARrpygkKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEAH--------------------SVG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 224 FFGPHlgmvyGKTEHLEGFTPYKVepakDVAPGrweTGTQSFEALAGFIAA----VDYI--------------------- 278
Cdd:cd06454   175 VYGPH-----GRGVEEFGGLTDDV----DIIMG---TLGKAFGAVGGYIAGskelIDYLrsyargfifstslppavaaaa 242

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1222443639 279 -AAISELDDSHSRREKLR--VAFAKTKQHEM 306
Cdd:cd06454   243 lAALEVLQGGPERRERLQenVRYLRRGLKEL 273
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 150-239 1.33e-05

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 46.81  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 150 DMAHFESLLNSNTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPhelIDVQALDC--DFLACSAYKFFGP 227
Cdd:cd00614   114 DPEALEAAIKPETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATP---YLQRPLELgaDIVVHSATKYIGG 190

                          90
                  ....*....|....*.
gi 1222443639 228 H----LGMVYGKTEHL 239
Cdd:cd00614   191 HsdviAGVVVGSGEAL 206
PLN02509 PLN02509
cystathionine beta-lyase
 87-234 2.75e-05

cystathionine beta-lyase


Pssm-ID: 178125 [Multi-domain]  Cd Length: 464  Bit Score: 46.18  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639  87 FGPNMTSLTfsfsrAISRNWQAGDEIIVTNADHFSNVSSWQQAAEDKGVVV---NTALVNEAdcsldmahfESLLNSNTK 163
Cdd:PLN02509  154 FTSGMAALS-----AVTHLIKNGEEIVAGDDVYGGSDRLLSQVVPRSGVVVkrvNTTNLDEV---------AAAIGPQTK 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222443639 164 LVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPhELIDVQALDCDFLACSAYKFFGPHLGMVYG 234
Cdd:PLN02509  220 LVWLESPTNPRQQISDIRKIAEMAHAQGALVLVDNSIMSP-VLSRPLELGADIVMHSATKFIAGHSDVMAG 289
PRK07324 PRK07324
transaminase; Validated
 150-200 6.56e-05

transaminase; Validated


Pssm-ID: 235989  Cd Length: 373  Bit Score: 44.54  E-value: 6.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1222443639 150 DMAHFESLLNSNTKLVAVTYASNTTGSIND---IKRIIELAHNVGALVYVDAVH 200
Cdd:PRK07324  142 DLDELRRLVRPNTKLICINNANNPTGALMDrayLEEIVEIARSVDAYVLSDEVY 195
MetC COG0626
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ...
 149-239 2.29e-04

Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440391 [Multi-domain]  Cd Length: 389  Bit Score: 43.11  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 149 LDMAHFESLLNSNTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDA-----VHYAPHElidvqaLDCDFLACSAYK 223
Cdd:COG0626   131 TDLAAVEAAIRPNTKLVFLETPSNPTLEVVDIAAIAAIAHAAGALLVVDNtfatpLLQRPLE------LGADIVVHSATK 204

                          90       100
                  ....*....|....*....|
gi 1222443639 224 FFGPH----LGMVYGKTEHL 239
Cdd:COG0626   205 YLGGHsdvlGGAVVGRDEEL 224
PRK07811 PRK07811
cystathionine gamma-synthase; Provisional
 150-234 4.88e-04

cystathionine gamma-synthase; Provisional


Pssm-ID: 236104 [Multi-domain]  Cd Length: 388  Bit Score: 41.94  E-value: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 150 DMAHFESLLNSNTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVD---AVHYAPHELidvqALDCDFLACSAYKFFG 226
Cdd:PRK07811  135 DLDAVRAAITPRTKLIWVETPTNPLLSITDIAALAELAHDAGAKVVVDntfASPYLQQPL----ALGADVVVHSTTKYIG 210


                  ....*...
gi 1222443639 227 PHLGMVYG 234
Cdd:PRK07811  211 GHSDVVGG 218
PRK08133 PRK08133
O-succinylhomoserine sulfhydrylase; Validated
 107-197 2.49e-03

O-succinylhomoserine sulfhydrylase; Validated


Pssm-ID: 181244 [Multi-domain]  Cd Length: 390  Bit Score: 39.60  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 107 QAGDEIIVTNADHFSNVSSWQQAAEDKGVvvNTALVNEADcsldMAHFESLLNSNTKLVAVTYASNTTGSINDIKRIIEL 186
Cdd:PRK08133   98 QAGDHVVSSRSLFGSTVSLFEKIFARFGI--ETTFVDLTD----LDAWRAAVRPNTKLFFLETPSNPLTELADIAALAEI 171

                          90
                  ....*....|.
gi 1222443639 187 AHNVGALVYVD 197
Cdd:PRK08133  172 AHAAGALLVVD 182
PRK07504 PRK07504
O-succinylhomoserine sulfhydrylase; Reviewed
 149-241 2.52e-03

O-succinylhomoserine sulfhydrylase; Reviewed


Pssm-ID: 168979 [Multi-domain]  Cd Length: 398  Bit Score: 39.74  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 149 LDMAHFESLLNSNTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPhelIDVQALDcdflacsaykfFGPH 228
Cdd:PRK07504  138 LDLDNWEKAVRPNTKVFFLESPTNPTLEVIDIAAVAKIANQAGAKLVVDNVFATP---LFQKPLE-----------LGAH 203

                          90
                  ....*....|...
gi 1222443639 229 LgMVYGKTEHLEG 241
Cdd:PRK07504  204 I-VVYSATKHIDG 215
GcvP2 COG1003
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ...
 110-197 3.03e-03

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: 39.63  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 110 DEIIVTNADHFSNVSSWQQAaedkG---VVVNTAlvneADCSLDMAHFESLLNSNTKLVAVTYAsNTTGSIN-DIKRIIE 185
Cdd:COG1003   142 NEILIPDSAHGTNPASAAMA----GfkvVVVKSD----EDGNVDLEDLKAKVGDRTAALMLTNP-STHGVFEeDIKEICD 212

                          90
                  ....*....|..
gi 1222443639 186 LAHNVGALVYVD 197
Cdd:COG1003   213 IVHEAGGLVYYD 224
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 145-228 5.86e-03

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 38.54  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 145 ADCSlDMAHFESLLNSNTKLVAVTYASNTTGSINDIKRIIELAHNVGALVYVDAVHYAPHeLIDVQALDCDFLACSAYKF 224
Cdd:PRK05994  133 ADAD-DPASFERAITPRTKAIFIESIANPGGTVTDIAAIAEVAHRAGLPLIVDNTLASPY-LIRPIEHGADIVVHSLTKF 210


                  ....
gi 1222443639 225 FGPH 228
Cdd:PRK05994  211 LGGH 214
PRK06234 PRK06234
methionine gamma-lyase; Provisional
 155-237 9.35e-03

methionine gamma-lyase; Provisional


Pssm-ID: 168478 [Multi-domain]  Cd Length: 400  Bit Score: 37.88  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443639 155 ESLLNSNTKLVAVTYASNTTGSINDIKRIIELAH--NVGALVYVDAVHYAPHELIDVQaLDCDFLACSAYKFFGPH---- 228
Cdd:PRK06234  143 RNALKANTKVVYLETPANPTLKVTDIKAISNIAHenNKECLVFVDNTFCTPYIQRPLQ-LGADVVVHSATKYLNGHgdvi 221


                  ....*....
gi 1222443639 229 LGMVYGKTE 237
Cdd:PRK06234  222 AGFVVGKEE 230
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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