ID B7HUX0_BACC7 Unreviewed; 406 AA.
AC B7HUX0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
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:ACJ80855.1};
GN OrderedLocusNames=BCAH187_A5121 {ECO:0000313|EMBL:ACJ80855.1};
OS Bacillus cereus (strain AH187).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534 {ECO:0000313|EMBL:ACJ80855.1, ECO:0000313|Proteomes:UP000002214};
RN [1] {ECO:0000313|EMBL:ACJ80855.1, ECO:0000313|Proteomes:UP000002214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187 {ECO:0000313|EMBL:ACJ80855.1,
RC ECO:0000313|Proteomes:UP000002214};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) 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}.
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DR EMBL; CP001177; ACJ80855.1; -; Genomic_DNA.
DR AlphaFoldDB; B7HUX0; -.
DR KEGG; bcr:BCAH187_A5121; -.
DR HOGENOM; CLU_003433_2_5_9; -.
DR Proteomes; UP000002214; Chromosome.
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 Transferase {ECO:0000256|RuleBase:RU004506, ECO:0000313|EMBL:ACJ80855.1}.
FT DOMAIN 23..391
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 406 AA; 45283 MW; 8532A7590F026D18 CRC64;
MNIHEIRKQF PILDQKVNGK QLVYFDSAAT SQKPIQVIET LERYYKEYNS NVHRGVHTLG
TKATDAYEGA REKVRKFINA KSMEEIIFTR GTTTALNTVA ASYGLENVKE GDEIVISYME
HHSNIIPWQQ VAKKTGATLK YLPLQPDGTI SLEDVRQTVT PNTKIVSIMY VSNVLGTINP
VKEIGAIAHE NGAIMVVDGA QSTPHMKVDV QDLNCDFYAL SAHKMCGPTG IGVLYGKKEL
LNNMEPIEFG GEMIDFVDLQ ESTWKELPWK FEAGTPIIGN AIGLGAAIDF LEEIGLDNIE
KHEHELAQYA LERLSEVDGV TIYGPKHRAG LVTFNIEDVH PHDVATVLDV EGIAVRAGHH
CAQPLMKWLK ASSTARASFY LYNTKEEIDT FVESLIKTKE YFTNVI
//
