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Database: UniProt
Entry: A0A3M8P6K0_9BACL
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ID   A0A3M8P6K0_9BACL        Unreviewed;       409 AA.
AC   A0A3M8P6K0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
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   ORFNames=EEX84_09480 {ECO:0000313|EMBL:RNF39309.1};
OS   Planococcus salinus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=1848460 {ECO:0000313|EMBL:RNF39309.1, ECO:0000313|Proteomes:UP000275473};
RN   [1] {ECO:0000313|EMBL:RNF39309.1, ECO:0000313|Proteomes:UP000275473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCB217 {ECO:0000313|EMBL:RNF39309.1,
RC   ECO:0000313|Proteomes:UP000275473};
RX   PubMed=29300160; DOI=10.1099/ijsem.0.002548;
RA   Gan L.;
RT   "Planococcus salinus sp. nov., a moderately halophilic bacterium isolated
RT   from a saline-alkali soil.";
RL   Int. J. Syst. Evol. Microbiol. 68:589-595(2018).
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:RNF39309.1}.
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DR   EMBL; RIAX01000006; RNF39309.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8P6K0; -.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000275473; 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:UP000275473};
KW   Transferase {ECO:0000256|RuleBase:RU004506}.
FT   DOMAIN          23..394
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   409 AA;  45420 MW;  59701E66E5E39FD4 CRC64;
     MINQEIKSYF PILNQEINGH PLVYLDSAAT SQKPVQVIEA LKKYYEFDNS NVHRGVHTLG
     NRATEHYEGA REKVQKFINA DSTEEIVFVR GTTTAINTIA QSYGRANVEE GDEIVITYME
     HHSNIIPWQQ LAKERGAILK YVELEEDGTI SLEQVRAAVT ERTKIVSMVY VSNVLGTMNP
     VKEVAQIAHE NGAVLVVDGA QAAPHLKIDV QQLDCDFFAF SGHKMCGPTG IGVMYGKKAL
     LNNMEPVEFG GEMIDFVGLY DSTWKELPWK FEGGTPIIAG AVALGAAIDF LNEIGLNEIE
     KHEHEMAAYA MNEMQQIKGL DIYGPKDPGK RAGIVTFNLK EVHPHDVATV LDMSGIAVRA
     GHHCAQPLMK WLDVTATARA SFYLYNNEAD VDRLVEGLRS AKEYFSDVF
//
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