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Conserved domains on  [gi|10383773|ref|NP_009912|]
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cysteine desulfurase [Saccharomyces cerevisiae S288C]

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) ...
 99-497 0e+00

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 PRK14012:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 404  Bit Score: 705.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   99 PIYLDMQATTPTDPRVLDTMLKFYT--GLYGNPHSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVL 176
Cdd:PRK14012   4 PIYLDYSATTPVDPRVAEKMMPYLTmdGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  177 KGVPRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPI 256
Cdd:PRK14012  84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  257 KEIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGGQERGLRSGT 336
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  337 LAPPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPDHRYPGCVNVSFAYVEGESLLMALRDIALS 416
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAVS 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  417 SGSACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSDRVKFLRELSPLWEMVQEGIDLNSIKWSG 496
Cdd:PRK14012 324 SGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWAH 403


                 .
gi 10383773  497 H 497
Cdd:PRK14012 404 H 404
 
Name Accession Description Interval E-value
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
99-497 0e+00

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 705.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   99 PIYLDMQATTPTDPRVLDTMLKFYT--GLYGNPHSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVL 176
Cdd:PRK14012   4 PIYLDYSATTPVDPRVAEKMMPYLTmdGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  177 KGVPRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPI 256
Cdd:PRK14012  84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  257 KEIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGGQERGLRSGT 336
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  337 LAPPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPDHRYPGCVNVSFAYVEGESLLMALRDIALS 416
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAVS 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  417 SGSACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSDRVKFLRELSPLWEMVQEGIDLNSIKWSG 496
Cdd:PRK14012 324 SGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWAH 403


                 .
gi 10383773  497 H 497
Cdd:PRK14012 404 H 404
IscS TIGR02006
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ...
 99-497 0e+00

cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases from a larger protein family designated (misleadingly, in this case) class V aminotransferases. IscS is one of at least 6 enzymes characteristic of the IscSUA-hscAB-fsx system of iron-sulfur cluster assembly. Scoring almost as well as proteobacterial sequences included in the model are mitochondrial cysteine desulfurases, apparently from an analogous system in eukaryotes. The sulfur, taken from cysteine, may be used in other systems as well, such as tRNA base modification and biosynthesis of other cofactors. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 131061 [Multi-domain]  Cd Length: 402  Bit Score: 641.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773    99 PIYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVLKG 178
Cdd:TIGR02006   4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   179 VPRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIKE 258
Cdd:TIGR02006  84 IAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   259 IGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGGQERGLRSGTLA 338
Cdd:TIGR02006 164 IGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTLP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   339 PPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPDHRYPGCVNVSFAYVEGESLLMALRDIALSSG 418
Cdd:TIGR02006 244 THQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSSG 323

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10383773   419 SACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSDRVKFLRELSPLWEMVQEGIDLNSIKWSGH 497
Cdd:TIGR02006 324 SACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH 402
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 98-477 0e+00

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: 620.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  98 RPIYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSnTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVLK 177
Cdd:COG1104   2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 178 GVPRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIK 257
Cdd:COG1104  81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 258 EIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRrpRVRLEPLLSGGGQERGLRSGTL 337
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGTE 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 338 APPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSA-EHTTLNGSPDHRYPGCVNVSFAYVEGESLLMAL--RDIA 414
Cdd:COG1104 239 NVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAiPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGIA 318

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10383773 415 LSSGSACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSDRVKFLRELS 477
Cdd:COG1104 319 VSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 100-462 1.80e-134

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: 393.15  E-value: 1.80e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   100 IYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINA-DPKEIIFTSGATESNNMVLKG 178
Cdd:pfam00266   1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   179 VPRFYKKtKKHIITTRTEHKCVLEAA-RAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIK 257
Cdd:pfam00266  81 LGRSLKP-GDEIVITEMEHHANLVPWqELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   258 EIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGG-------QER 330
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQES 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   331 GL-------RSGTLAPPLVAGFGEAAR-LMKKEFDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPdhRYPGCVNVSFAYVE 402
Cdd:pfam00266 240 TFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNFKGVH 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10383773   403 GESLLMALRD--IALSSGSACTsaslEPSYVLHALgkddalaHSSIRFGIGRFSTEEEVDYV 462
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDRL 368
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 100-466 5.82e-73

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: 235.44  E-value: 5.82e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 100 IYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINA-DPKEIIFTSGATESNNMVLKG 178
Cdd:cd06453   1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 179 VPRFYKKtKKHIITTRTEHKCVL----EAARammKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQ 254
Cdd:cd06453  81 LGRANKP-GDEIVTSVMEHHSNIvpwqQLAE---RTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTIN 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 255 PIKEIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGGQERG--- 331
Cdd:cd06453 157 PVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEvsf 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 332 -----------LRSGTLAPPLVAGFGEAARLMKKE-FDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPDHRYPGcvnVSFA 399
Cdd:cd06453 237 eettyadlphkFEAGTPNIAGAIGLGAAIDYLEKIgMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAGV---VSFN 313

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10383773 400 yVEG---ESLLMAL--RDIALSSGSACTsaslEPsyVLHALGKddalaHSSIRFGIGRFSTEEEVDYVVKAV 466
Cdd:cd06453 314 -LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLGV-----PGTVRASFGLYNTEEEIDALVEAL 373
f2_encap_cargo1 NF041166
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ...
 98-313 4.46e-18

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: 87.22  E-value: 4.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   98 RP-IYLDMQATTpTDPR-VLDTMLKFYTglygnpH--SNTHSYGWE-----TNtAVENARAHVAKMINA-DPKEIIFTSG 167
Cdd:NF041166 244 KPlVWFDNAATT-QKPQaVIDRLSYFYE------HenSNIHRAAHElaaraTD-AYEGAREKVRRFIGApSVDEIIFVRG 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  168 ATESNNMVLK--GvprfykktKKH------IITTRTEHKC--V---LEAAR--AMMKegfeVtfLNVDDQGLIDLKELED 232
Cdd:NF041166 316 TTEAINLVAKswG--------RQNigagdeIIVSHLEHHAniVpwqQLAQEtgAKLR----V--IPVDDSGQILLDEYAK 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  233 AIRPDTCLVSVMAVNNEIGVIQPIKEIGAICrknkiyfH-------TDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKG 305
Cdd:NF041166 382 LLNPRTKLVSVTQVSNALGTVTPVKEIIALA-------HragakvlVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTG 454


                 ....*...
gi 10383773  306 IGAIYVRR 313
Cdd:NF041166 455 IGVVYGKR 462
 
Name Accession Description Interval E-value
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
99-497 0e+00

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 705.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   99 PIYLDMQATTPTDPRVLDTMLKFYT--GLYGNPHSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVL 176
Cdd:PRK14012   4 PIYLDYSATTPVDPRVAEKMMPYLTmdGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  177 KGVPRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPI 256
Cdd:PRK14012  84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  257 KEIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGGQERGLRSGT 336
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGT 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  337 LAPPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPDHRYPGCVNVSFAYVEGESLLMALRDIALS 416
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDLAVS 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  417 SGSACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSDRVKFLRELSPLWEMVQEGIDLNSIKWSG 496
Cdd:PRK14012 324 SGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIEWAH 403


                 .
gi 10383773  497 H 497
Cdd:PRK14012 404 H 404
IscS TIGR02006
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ...
 99-497 0e+00

cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases from a larger protein family designated (misleadingly, in this case) class V aminotransferases. IscS is one of at least 6 enzymes characteristic of the IscSUA-hscAB-fsx system of iron-sulfur cluster assembly. Scoring almost as well as proteobacterial sequences included in the model are mitochondrial cysteine desulfurases, apparently from an analogous system in eukaryotes. The sulfur, taken from cysteine, may be used in other systems as well, such as tRNA base modification and biosynthesis of other cofactors. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 131061 [Multi-domain]  Cd Length: 402  Bit Score: 641.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773    99 PIYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVLKG 178
Cdd:TIGR02006   4 PIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLAIKG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   179 VPRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIKE 258
Cdd:TIGR02006  84 IAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQDIAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   259 IGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGGQERGLRSGTLA 338
Cdd:TIGR02006 164 IGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSGTLP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   339 PPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPDHRYPGCVNVSFAYVEGESLLMALRDIALSSG 418
Cdd:TIGR02006 244 THQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAVSSG 323

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10383773   419 SACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSDRVKFLRELSPLWEMVQEGIDLNSIKWSGH 497
Cdd:TIGR02006 324 SACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWAAH 402
PLN02651 PLN02651
cysteine desulfurase
 100-460 0e+00

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 626.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  100 IYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVLKGV 179
Cdd:PLN02651   1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  180 PRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIKEI 259
Cdd:PLN02651  81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  260 GAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGGQERGLRSGTLAP 339
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTENT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  340 PLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSA-EHTTLNG--SPDHRYPGCVNVSFAYVEGESLLMALRDIALS 416
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKlGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMGLKEVAVS 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 10383773  417 SGSACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVD 460
Cdd:PLN02651 321 SGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 98-477 0e+00

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: 620.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  98 RPIYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSnTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVLK 177
Cdd:COG1104   2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 178 GVPRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIK 257
Cdd:COG1104  81 GAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 258 EIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRrpRVRLEPLLSGGGQERGLRSGTL 337
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGTE 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 338 APPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSA-EHTTLNGSPDHRYPGCVNVSFAYVEGESLLMAL--RDIA 414
Cdd:COG1104 239 NVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAiPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGIA 318

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10383773 415 LSSGSACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSDRVKFLRELS 477
Cdd:COG1104 319 VSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
FeS_nifS TIGR03402
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ...
 100-479 9.43e-175

cysteine desulfurase NifS; Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403.


Pssm-ID: 132443 [Multi-domain]  Cd Length: 379  Bit Score: 495.98  E-value: 9.43e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   100 IYLDMQATTPTDPRVLDTMLKFYTGLYGNPhSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVLKGV 179
Cdd:TIGR03402   1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNP-SSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   180 PRFYKKtKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIKEI 259
Cdd:TIGR03402  80 LAAQPE-KRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   260 GAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRrpRVRLEPLLSGGGQERGLRSGTLAP 339
Cdd:TIGR03402 159 GEIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRK--GTRFRPLLRGGHQERGRRAGTENV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   340 PLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSA-EHTTLNGSPDHRYPGCVNVSFAYVEGESLLMALRD--IALS 416
Cdd:TIGR03402 237 PGIVGLGKAAELATEHLEEENTRVRALRDRLEAGLLARiPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLDMegICAS 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10383773   417 SGSACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSDRVKFLRELSPL 479
Cdd:TIGR03402 317 SGSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMSPF 379
DNA_S_dndA TIGR03235
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ...
 101-448 4.14e-152

cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a larger family of cysteine desulfurases. It is encoded, typically, divergently from a conserved, sparsely distributed operon for sulfur modification of DNA. This modification system is designated dnd, after the phenotype of DNA degradation during electrophoresis. The system is sporadically distributed in bacteria, much like some restriction enzyme operons. DndB is described as a putative ATPase. [DNA metabolism, Restriction/modification]


Pssm-ID: 163191 [Multi-domain]  Cd Length: 353  Bit Score: 437.69  E-value: 4.14e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   101 YLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVLKGVP 180
Cdd:TIGR03235   1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRTHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   181 RFYKKT-KKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIKEI 259
Cdd:TIGR03235  81 RAGEQKgKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   260 GAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRR--PRVRLEPLLSGGGQERGLRSGTL 337
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRgkPKAPLKPIMFGGGQERGLRPGTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   338 APPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGlLSAEHTTLNGSPDHRYPGCVNVSFAYVEGESLLMALR-DIALS 416
Cdd:TIGR03235 241 PVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDA-LQTLGVKLNGDPAETIPHILNFSIDGVNSEALIVNLRaDAAVS 319

                         330       340       350
                  ....*....|....*....|....*....|..
gi 10383773   417 SGSACTSASLEPSYVLHALGKDDALAHSSIRF 448
Cdd:TIGR03235 320 TGSACSSSKYEPSHVLQAMGLDTDRARGAIRF 351
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 100-462 1.80e-134

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: 393.15  E-value: 1.80e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   100 IYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINA-DPKEIIFTSGATESNNMVLKG 178
Cdd:pfam00266   1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   179 VPRFYKKtKKHIITTRTEHKCVLEAA-RAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIK 257
Cdd:pfam00266  81 LGRSLKP-GDEIVITEMEHHANLVPWqELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   258 EIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGG-------QER 330
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQES 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   331 GL-------RSGTLAPPLVAGFGEAAR-LMKKEFDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPdhRYPGCVNVSFAYVE 402
Cdd:pfam00266 240 TFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNFKGVH 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10383773   403 GESLLMALRD--IALSSGSACTsaslEPSYVLHALgkddalaHSSIRFGIGRFSTEEEVDYV 462
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVDRL 368
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
100-468 1.71e-103

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 314.75  E-value: 1.71e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  100 IYLDMQATTPTDPRVLDTMLKFYTGLYGNpHSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVLKGV 179
Cdd:PRK02948   2 IYLDYAATTPMSKEALQTYQKAASQYFGN-ESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  180 PRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIKEI 259
Cdd:PRK02948  81 LNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  260 GAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVrrRPRVRLEPLLSGGGQERGLRSGTLAP 339
Cdd:PRK02948 161 GALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYI--NPQVRWKPVFPGTTHEKGFRPGTVNV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  340 PLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSAE-HTTLNGSPDHRYPGCVNVSFAYVEGESLLMAL--RDIALS 416
Cdd:PRK02948 239 PGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPlPIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECnrRGIAIS 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10383773  417 SGSACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSD 468
Cdd:PRK02948 319 TGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHALET 370
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
94-472 5.71e-78

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 249.29  E-value: 5.71e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  94 GFGTRPIYLDMQATTPTdPR-VLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINA-DPKEIIFTSGATES 171
Cdd:COG0520  11 VLGKPLVYLDNAATGQK-PRpVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTEA 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 172 NNMVLKGVPRFykKTKKHIITTRTEHKCVLEAARAMMKE-GFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEI 250
Cdd:COG0520  90 INLVAYGLGRL--KPGDEILITEMEHHSNIVPWQELAERtGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVT 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 251 GVIQPIKEIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGG--- 327
Cdd:COG0520 168 GTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPPFLGGGGmie 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 328 ---------QERGLR--SGTLAPPLVAGFGEAARLMKK-EFDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPDHRYPGCVn 395
Cdd:COG0520 248 wvsfdgttyADLPRRfeAGTPNIAGAIGLGAAIDYLEAiGMEAIEARERELTAYALEGLAAIPGVRILGPADPEDRSGI- 326

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 396 VSFaYVEG---ESLLMALRD--IALSSGSACTsaslEPsyVLHALGKDdalahSSIRFGIGRFSTEEEVDYVVKAVSDRV 470
Cdd:COG0520 327 VSF-NVDGvhpHDVAALLDDegIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFHLYNTEEEIDRLVEALKKLA 394


                ..
gi 10383773 471 KF 472
Cdd:COG0520 395 EL 396
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 100-466 5.82e-73

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: 235.44  E-value: 5.82e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 100 IYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINA-DPKEIIFTSGATESNNMVLKG 178
Cdd:cd06453   1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 179 VPRFYKKtKKHIITTRTEHKCVL----EAARammKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQ 254
Cdd:cd06453  81 LGRANKP-GDEIVTSVMEHHSNIvpwqQLAE---RTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTIN 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 255 PIKEIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGGQERG--- 331
Cdd:cd06453 157 PVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEvsf 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 332 -----------LRSGTLAPPLVAGFGEAARLMKKE-FDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPDHRYPGcvnVSFA 399
Cdd:cd06453 237 eettyadlphkFEAGTPNIAGAIGLGAAIDYLEKIgMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAGV---VSFN 313

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10383773 400 yVEG---ESLLMAL--RDIALSSGSACTsaslEPsyVLHALGKddalaHSSIRFGIGRFSTEEEVDYVVKAV 466
Cdd:cd06453 314 -LEGihpHDVATILdqYGIAVRAGHHCA----QP--LMRRLGV-----PGTVRASFGLYNTEEEIDALVEAL 373
PLN02855 PLN02855
Bifunctional selenocysteine lyase/cysteine desulfurase
 71-476 6.01e-37

Bifunctional selenocysteine lyase/cysteine desulfurase


Pssm-ID: 215460 [Multi-domain]  Cd Length: 424  Bit Score: 141.04  E-value: 6.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   71 GTTPDAvvASGSTAMSHAYQENTGF------GTRPIYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAV 144
Cdd:PLN02855   1 SSAPAA--SAASVSLGAETRPDFPIldqtvnGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  145 ENARAHVAKMINA-DPKEIIFTSGATESNNMVLKGVPRFYKKTKKHIITTRTE-HKCVLEAARAMMKEGFEVTFLNVDDQ 222
Cdd:PLN02855  79 ELARKKVAAFINAsTSREIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEhHSNIVPWQLVAQKTGAVLKFVGLTPD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  223 GLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIKEIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYG 302
Cdd:PLN02855 159 EVLDVEQLKELLSEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  303 PKGIGAIYVRRRPRVRLEPLLSGGG--QERGLRSGTLAPP------------LVAGFGEAAR-LMKKEFDNDQAHIKRLS 367
Cdd:PLN02855 239 PTGIGFLWGKSDLLESMPPFLGGGEmiSDVFLDHSTYAPPpsrfeagtpaigEAIGLGAAIDyLSEIGMDRIHEYEVELG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  368 DKLVKGLLSAEHTTLNGSP----DHRYPGCvnvSFAyVEG------ESLLMALRDIALSSGSACTsaslEPsyvLH-ALG 436
Cdd:PLN02855 319 TYLYEKLSSVPGVRIYGPKpsegVGRAALC---AFN-VEGihptdlSTFLDQQHGVAIRSGHHCA----QP---LHrYLG 387

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 10383773  437 KdDALAHSSIRFgigrFSTEEEVDYVVKAVSDRVKFLREL 476
Cdd:PLN02855 388 V-NASARASLYF----YNTKEEVDAFIHALKDTIAFFSSF 422
PRK09295 PRK09295
cysteine desulfurase SufS;
100-326 1.16e-25

cysteine desulfurase SufS;


Pssm-ID: 181766 [Multi-domain]  Cd Length: 406  Bit Score: 108.69  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  100 IYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINA-DPKEIIFTSGATESNNMVLKG 178
Cdd:PRK09295  25 AYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINLVANS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  179 VPRFYKKTKKHIITTRTEHKCVLEAARAMMKE-GFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIK 257
Cdd:PRK09295 105 WGNSNVRAGDNIIISEMEHHANIVPWQMLCARvGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENPLA 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10383773  258 EIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGG 326
Cdd:PRK09295 185 EMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMPPWEGGG 253
PRK10874 PRK10874
cysteine desulfurase CsdA;
100-475 9.01e-25

cysteine desulfurase CsdA;


Pssm-ID: 182799 [Multi-domain]  Cd Length: 401  Bit Score: 105.89  E-value: 9.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  100 IYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINA-DPKEIIFTSGATESNNMVLKG 178
Cdd:PRK10874  21 VYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVAQS 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  179 VPRFYKKTKKHIITTRTEHKCVLeAARAMMKE--GFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPI 256
Cdd:PRK10874 101 YARPRLQPGDEIIVSEAEHHANL-VPWLMVAQqtGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPDL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  257 KEIGAICRKNKIYFHTDAAQayGKIH--IDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGG------- 327
Cdd:PRK10874 180 ARAITLAHQAGMVVMVDGAQ--GAVHfpADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSPWQGGGKmltevsf 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  328 -----QE--RGLRSGTlapPLVAG-FGEAARL-MKKEFDNDQAhikrlsDKLVKGLLSAEHTTLNGSPDHRYPGCVNVS- 397
Cdd:PRK10874 258 dgftpQSapWRFEAGT---PNVAGvIGLSAALeWLADIDINQA------ESWSRSLATLAEDALAKLPGFRSFRCQDSSl 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  398 ----FAYVEGESL--LMALRDIALSSGSACTsaslEPsyVLHALGKDDALahssiRFGIGRFSTEEEVDYVVKAVSDRVK 471
Cdd:PRK10874 329 lafdFAGVHHSDLvtLLAEYGIALRAGQHCA----QP--LLAALGVTGTL-----RASFAPYNTQSDVDALVNAVDRALE 397


                 ....
gi 10383773  472 FLRE 475
Cdd:PRK10874 398 LLVD 401
f2_encap_cargo1 NF041166
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ...
 98-313 4.46e-18

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: 87.22  E-value: 4.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   98 RP-IYLDMQATTpTDPR-VLDTMLKFYTglygnpH--SNTHSYGWE-----TNtAVENARAHVAKMINA-DPKEIIFTSG 167
Cdd:NF041166 244 KPlVWFDNAATT-QKPQaVIDRLSYFYE------HenSNIHRAAHElaaraTD-AYEGAREKVRRFIGApSVDEIIFVRG 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  168 ATESNNMVLK--GvprfykktKKH------IITTRTEHKC--V---LEAAR--AMMKegfeVtfLNVDDQGLIDLKELED 232
Cdd:NF041166 316 TTEAINLVAKswG--------RQNigagdeIIVSHLEHHAniVpwqQLAQEtgAKLR----V--IPVDDSGQILLDEYAK 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  233 AIRPDTCLVSVMAVNNEIGVIQPIKEIGAICrknkiyfH-------TDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKG 305
Cdd:NF041166 382 LLNPRTKLVSVTQVSNALGTVTPVKEIIALA-------HragakvlVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTG 454


                 ....*...
gi 10383773  306 IGAIYVRR 313
Cdd:NF041166 455 IGVVYGKR 462
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 144-312 8.63e-17

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 77.81  E-value: 8.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 144 VENARAHVAKMINADPKEIIFTSGATESNNMVLKgvprFYKKTKKHIITTRTEHKCVLEAARAMmkEGFEVTFLNVDD-- 221
Cdd:cd01494   2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAALL----ALLGPGDEVIVDANGHGSRYWVAAEL--AGAKPVPVPVDDag 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 222 QGLIDLKELED-AIRPDTCLVSVMAVNNEIGVIQPIKEIGAICRKNKIYFHTDAAQAYG---KIHIDVNEMNIDLLSISS 297
Cdd:cd01494  76 YGGLDVAILEElKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGaspAPGVLIPEGGADVVTFSL 155

                       170
                ....*....|....*
gi 10383773 298 HKIYGPKGIGAIYVR 312
Cdd:cd01494 156 HKNLGGEGGGVVIVK 170
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 132-312 2.16e-15

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: 77.24  E-value: 2.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 132 NTHSYGWETNTAVENARAHV----AKMINADPKEI--IFTSGATESNNMVLKGVPRFYKKTKKH----------IITTRT 195
Cdd:cd06450  24 NAIDFTWDESPAATEMEAEVvnwlAKLFGLPSEDAdgVFTSGGSESNLLALLAARDRARKRLKAgggrgidklvIVCSDQ 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 196 EHKCVLEAARAMMKEgfeVTFLNVDDQGLIDLKELEDAIRPD------TCLVSVMAVNNEIGVIQPIKEIGAICRKNKIY 269
Cdd:cd06450 104 AHVSVEKAAAYLDVK---VRLVPVDEDGRMDPEALEAAIDEDkaeglnPIMVVATAGTTDTGAIDPLEEIADLAEKYDLW 180

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 10383773 270 FHTDAaqAYG--------KIHIDVNEMNIDLLSISSHKiYG--PKGIGAIYVR 312
Cdd:cd06450 181 LHVDA--AYGgfllpfpePRHLDFGIERVDSISVDPHK-YGlvPLGCSAVLVR 230
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 163-314 5.31e-12

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 67.55  E-value: 5.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 163 IFTSGATESNnMV------------------LKGVPRFykktkkHIITTRTEHKCVLEAARAMmkeGFE---VTFLNVDD 221
Cdd:COG0076 129 VFTSGGTEAN-LLallaardralarrvraegLPGAPRP------RIVVSEEAHSSVDKAARLL---GLGrdaLRKVPVDE 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 222 QGLIDLKELEDAIRPDT-------CLV-SVMAVNneIGVIQPIKEIGAICRKNKIYFHTDAaqAYG---------KIHID 284
Cdd:COG0076 199 DGRMDPDALEAAIDEDRaaglnpiAVVaTAGTTN--TGAIDPLAEIADIAREHGLWLHVDA--AYGgfalpspelRHLLD 274

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 10383773 285 ----VNEMNIDLlsissHKiYG--PKGIGAIYVRRR 314
Cdd:COG0076 275 gierADSITVDP-----HK-WLyvPYGCGAVLVRDP 304
PLN02724 PLN02724
Molybdenum cofactor sulfurase
 100-327 1.50e-08

Molybdenum cofactor sulfurase


Pssm-ID: 215384 [Multi-domain]  Cd Length: 805  Bit Score: 57.19  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  100 IYLDMQATTPTDPRVLDTMLKFYTG-LYGNPHSNTHSyGWETNTAVENARAHVAKMINADPKE--IIFTSGATESNNMVL 176
Cdd:PLN02724  36 VYLDHAGATLYSESQLEAALADFSSnVYGNPHSQSDS-SMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATAALKLVG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  177 KGVPRfykKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNV--------DDQGLIDLK----------------ELED 232
Cdd:PLN02724 115 ETFPW---SSESHFCYTLENHNSVLGIREYALEKGAAAIAVDIeeaanqptNSQGSVVVKsrglqrrntsklqkreDDGE 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  233 AIR----PDTCLVSVMAVNNEIgvIQPIKEIGAI--CRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYG-PKG 305
Cdd:PLN02724 192 AYNlfafPSECNFSGAKFPLDL--VKLIKDNQHSnfSKSGRWMVLLDAAKGCGTSPPDLSRYPADFVVVSFYKIFGyPTG 269

                        250       260
                 ....*....|....*....|..
gi 10383773  306 IGAIYVRRRPRVRLEPLLSGGG 327
Cdd:PLN02724 270 LGALLVRRDAAKLLKKKYFGGG 291
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
 211-313 1.74e-06

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 49.91  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  211 GFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEI--GVIQPIKEIGAICRKNKIYFHTDAAQAYGKIHIDVNEM 288
Cdd:PRK13479 103 GIAHVVLDTGEDEPPDAAEVEAALAADPRITHVALVHCETttGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPIDIAEL 182

                         90       100
                 ....*....|....*....|....*.
gi 10383773  289 NIDLLSISSHK-IYGPKGIGAIYVRR 313
Cdd:PRK13479 183 GIDALISSANKcIEGVPGFGFVIARR 208
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 211-374 1.77e-06

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: 49.98  E-value: 1.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 211 GFEVTFLNVDDQGLIDLKELEDAIRPDTcLVSVMAVNNE--IGVIQPIKEIGAICRKNKIYFHTDAAQAYGKIHIDVNEM 288
Cdd:cd06451  97 GADVDVVEKPWGEAVSPEEIAEALEQHD-IKAVTLTHNEtsTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEW 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 289 NIDLLSISSHKIYG-PKGIGAIYVRRRPRVRLEP-----------LLSGGGQERGLRS-GTLAPPLVAGFGEAARLMKKE 355
Cdd:cd06451 176 GVDVAYTGSQKALGaPPGLGPIAFSERALERIKKktkpkgfyfdlLLLLKYWGEGYSYpHTPPVNLLYALREALDLILEE 255

                       170       180
                ....*....|....*....|
gi 10383773 356 -FDNDQAHIKRLSDKLVKGL 374
Cdd:cd06451 256 gLENRWARHRRLAKALREGL 275
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
130-314 1.40e-05

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 47.41  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   130 HSNTHSYGWETN---TAVENARAH-VAKMINAdPKEI-------IFTSGATESNNMVLKGVP-RFYKKTKKH-------- 189
Cdd:pfam00282  63 AINCNGFTWESSpacTELENVVMNwLGEMLGL-PAEFlgqegggVLQPGSSESNLLALLAARtKWIKRMKAAgkpadssg 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   190 ------IITTRTEHKCVLEAARAMmkeGFEVTFLNVDDQGLIDLKELEDAIRPD-------TCLVSVMAVNNeIGVIQPI 256
Cdd:pfam00282 142 ilaklvAYTSDQAHSSIEKAALYG---GVKLREIPSDDNGKMRGMDLEKAIEEDkenglipFFVVATLGTTG-SGAFDDL 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10383773   257 KEIGAICRKNKIYFHTDAAQAYGKI------HIDVNEMNIDLLSISSHKIYG-PKGIGAIYVRRR 314
Cdd:pfam00282 218 QELGDICAKHNLWLHVDAAYGGSAFicpefrHWLFGIERADSITFNPHKWMLvLLDCSAVWVKDK 282
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
190-370 2.59e-05

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 46.05  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   190 IITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPD-------TCLVSV-MAVNNEIGVIQP---IKE 258
Cdd:pfam01212  74 VICGEPAHIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVgadifppTGLISLeNTHNSAGGQVVSlenLRE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   259 IGAICRKNKIYFHTDAAQ---AYGKIHIDVNEM--NIDLLSISshkiyGPKG----IGAI------YVRRRPRVRLepLL 323
Cdd:pfam01212 154 IAALAREHGIPVHLDGARfanAAVALGVIVKEItsYADSVTMC-----LSKGlgapVGSVlagsddFIAKAIRQRK--YL 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 10383773   324 SGGGQERGLrsgtlapPLVAGFGeAARLMKKEFDNDQAHIKRLSDKL 370
Cdd:pfam01212 227 GGGLRQAGV-------LAAAGLR-ALEEGVARLARDHATARRLAEGL 265
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 107-308 5.79e-05

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 45.02  E-value: 5.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 107 TTPTdPRVLDTMLKfytglygnphSNTHSYGWETNTAVENARAHVAKMINADpkEIIFTSGATESNNMVLKG-VPRFYKk 185
Cdd:cd06502   8 TGPT-PEMLEAMAA----------ANVGDDVYGEDPTTAKLEARAAELFGKE--AALFVPSGTAANQLALAAhTQPGGS- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 186 tkkhIITTRTEHKCVLEAARAMMKEGfeVTFLNVD-DQGLIDLKELEDAIRPDT----CLVSVMAVNN--EIGVIQP--- 255
Cdd:cd06502  74 ----VICHETAHIYTDEAGAPEFLSG--VKLLPVPgENGKLTPEDLEAAIRPRDdihfPPPSLVSLENttEGGTVYPlde 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10383773 256 IKEIGAICRKNKIYFHTD------AAQAYGkihidVNEMNI----DLLSISshkiyGPKGIGA 308
Cdd:cd06502 148 LKAISALAKENGLPLHLDgarlanAAAALG-----VALKTYksgvDSVSFC-----LSKGGGA 200
PRK05939 PRK05939
cystathionine gamma-synthase family protein;
211-273 2.20e-04

cystathionine gamma-synthase family protein;


Pssm-ID: 235650 [Multi-domain]  Cd Length: 397  Bit Score: 43.52  E-value: 2.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10383773  211 GFEVTFLNVddqglIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIKEIGAICRKNKIYFHTD 273
Cdd:PRK05939 110 GVEVTMVDA-----TDVQNVAAAIRPNTRMVFVETIANPGTQVADLAGIGALCRERGLLYVVD 167
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 155-269 3.52e-04

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 42.71  E-value: 3.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773 155 INADPKEIIFTSGATESNNMVLkgvpRFYKKTKKHIITTRTEHKCVLEAARAMmkeGFEVTFLNVDDQG--LIDLKELED 232
Cdd:cd00609  55 VDVPPEEIVVTNGAQEALSLLL----RALLNPGDEVLVPDPTYPGYEAAARLA---GAEVVPVPLDEEGgfLLDLELLEA 127

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 10383773 233 AIRPDTCLVSVMAVNNEIGVIQP---IKEIGAICRKNKIY 269
Cdd:cd00609 128 AKTPKTKLLYLNNPNNPTGAVLSeeeLEELAELAKKHGIL 167
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
206-302 2.26e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 40.44  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  206 AMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQP---IKEIGAICRKNKIYFHTDAAQAY---- 278
Cdd:PRK05957 129 AITMAGCQPILVPTDDNYQLQPEAIEQAITPKTRAIVTISPNNPTGVVYPealLRAVNQICAEHGIYHISDEAYEYftyd 208

                         90       100       110
                 ....*....|....*....|....*....|
gi 10383773  279 GKIHI------DVNEMNIDLLSISshKIYG 302
Cdd:PRK05957 209 GVKHFspgsipGSGNHTISLYSLS--KAYG 236
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 203-275 4.14e-03

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: 39.52  E-value: 4.14e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10383773 203 AARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTclVSVMAVN-NEIGVI-QPIKEIGAICRKNKIYFHTDAA 275
Cdd:cd00613 125 ARTRGEPLGIEVVEVPSDEGGTVDLEALKEEVSEEV--AALMVQYpNTLGVFeDLIKEIADIAHSAGALVYVDGD 197
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
107-374 6.39e-03

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 38.83  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   107 TTPTDPRVLDTMLKFYTGlygnphSNTHSYG-WETNTAVENArahVAKMINADPK-------EIIFTSGATESNNMVlkg 178
Cdd:pfam00155  12 LGDTLPAVAKAEKDALAG------GTRNLYGpTDGHPELREA---LAKFLGRSPVlkldreaAVVFGSGAGANIEAL--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   179 vPRFYKKTKKHIIT---TRTEHKCVLEAArammkeGFEVTFLNVDDQ--GLIDLKELEDAIRPDTCLVSVMAVNNEIGVI 253
Cdd:pfam00155  80 -IFLLANPGDAILVpapTYASYIRIARLA------GGEVVRYPLYDSndFHLDFDALEAALKEKPKVVLHTSPHNPTGTV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773   254 QP---IKEIGAICRKNKIY-FHTDA-------AQAYGKIHIDVNEMnIDLLSISS-HKIYGPKG--IGAIYVRRRPRVRL 319
Cdd:pfam00155 153 ATleeLEKLLDLAKEHNILlLVDEAyagfvfgSPDAVATRALLAEG-PNLLVVGSfSKAFGLAGwrVGYILGNAAVISQL 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 10383773   320 EPLLsgggqeRGLRSGTLAPPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGL 374
Cdd:pfam00155 232 RKLA------RPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGL 280
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
211-270 7.77e-03

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 38.58  E-value: 7.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10383773  211 GFEVTFLNVDDqGLIDLKELEDAIRPDTCLVsVMAVNNEIGVIQPIKEIGAICRKNKIYF 270
Cdd:PRK00451 179 GIEVVEVPYED-GVTDLEALEAAVDDDTAAV-VVQYPNFFGVIEDLEEIAEIAHAGGALF 236
 
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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