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Database: UniProt
Entry: C4GAH9_9FIRM
LinkDB: C4GAH9_9FIRM
Original site: C4GAH9_9FIRM 
ID   C4GAH9_9FIRM            Unreviewed;       415 AA.
AC   C4GAH9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN   Name=sufS {ECO:0000313|EMBL:EEP28122.1};
GN   ORFNames=GCWU000342_00930 {ECO:0000313|EMBL:EEP28122.1};
OS   Shuttleworthia satelles DSM 14600.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Shuttleworthia.
OX   NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP28122.1, ECO:0000313|Proteomes:UP000003494};
RN   [1] {ECO:0000313|EMBL:EEP28122.1, ECO:0000313|Proteomes:UP000003494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP28122.1,
RC   ECO:0000313|Proteomes:UP000003494};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC       from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC       produce L-alanine. {ECO:0000256|RuleBase:RU004506}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC         alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC         COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:64428; EC=2.8.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00001357,
CC         ECO:0000256|RuleBase:RU004506};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily. {ECO:0000256|ARBA:ARBA00010447,
CC       ECO:0000256|RuleBase:RU004506}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEP28122.1}.
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DR   EMBL; ACIP02000002; EEP28122.1; -; Genomic_DNA.
DR   RefSeq; WP_006905941.1; NZ_GG665866.1.
DR   AlphaFoldDB; C4GAH9; -.
DR   STRING; 626523.GCWU000342_00930; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_9; -.
DR   Proteomes; UP000003494; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06453; SufS_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01979; sufS; 1.
DR   PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003494};
KW   Transferase {ECO:0000256|RuleBase:RU004506}.
FT   DOMAIN          21..399
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   415 AA;  46195 MW;  65C3A205153411EC CRC64;
     MTDEEKRIRA DFPLLANRDI VYLDNSATTQ KPQSVLEVDL SFYQKRNANP LRGLYQLSID
     ATDAYEGARA KVADFIGAGR PEEIVFTRNA TEALNLVAYS YGRSFLKEGD EIVLSVAEHH
     SNILPWQGVA QATGARLVWF ECDDTGKLDP ERLRELVNEH TKIVAISQVS NVFGRSNDAG
     EYARIAHEAG AVYVCDGAQS VPHMPVDVRE MDCDFLAFSG HKMLSAMGIG VLYARYELLE
     KMPPFMTGGE MIEYVTREGA TYAEIPHKFE AGTVNAGGAV SLAAAIDYYH KIGFETIQRR
     EEDLSVYMME GMKKIPHIHI LGSEDPTDHH GIVTFTIDGV HPHDVAAIFD ASGICVRAGH
     HCAQPLHRHL TKISEKVAYM STTRASLAFY NTREDVDRFL TCLADIRREM GYGNE
//
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