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Database: UniProt
Entry: A0A0M9DKP9_9BACI
LinkDB: A0A0M9DKP9_9BACI
Original site: A0A0M9DKP9_9BACI 
ID   A0A0M9DKP9_9BACI        Unreviewed;       409 AA.
AC   A0A0M9DKP9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=ADM90_10820 {ECO:0000313|EMBL:KOY82132.1};
OS   Lysinibacillus macroides.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=33935 {ECO:0000313|EMBL:KOY82132.1, ECO:0000313|Proteomes:UP000037977};
RN   [1] {ECO:0000313|EMBL:KOY82132.1, ECO:0000313|Proteomes:UP000037977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 54 {ECO:0000313|EMBL:KOY82132.1,
RC   ECO:0000313|Proteomes:UP000037977};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA   Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (JUL-2015) 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:KOY82132.1}.
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DR   EMBL; LGCI01000006; KOY82132.1; -; Genomic_DNA.
DR   RefSeq; WP_053995033.1; NZ_LGCI01000006.1.
DR   AlphaFoldDB; A0A0M9DKP9; -.
DR   STRING; 33935.ADM90_10820; -.
DR   PATRIC; fig|33935.3.peg.4071; -.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000037977; 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   Transferase {ECO:0000256|RuleBase:RU004506}.
FT   DOMAIN          23..394
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   409 AA;  45033 MW;  DB269051054DE15E CRC64;
     MMNKDIKSYF PILNQDVNGH RLVYLDSAAT SQKPVQVIEA IKSYYEFDNS NVHRGVHTLG
     NRATDRYEGA REKVRKFIHA MSTQEIIFTR GTTTSLNTVA ASYGRANVAE GDEIVITQME
     HHSNIIPWQQ LAKEKKATLK YIELEADGTI SLEKVRATIT PQTKIVAVSM ASNVLGTINP
     IKEIAQIAHA NGAVMVADGA QAAPHMKIDV QDLDVDFLGF SGHKMCGPTG IGVLYGKKEH
     LEKMEPVEFG GEMIDFVGLY DSTWKELPWK FEGGTPIIAG AIGLGAAIDF LTDIGLDTIA
     AHEHKLVGYA MDQLETIDGL KIFGPRDPMK RCGLVTFNLD DVHPHDVATV LDMNGIAIRA
     GHHCAQPLMK CLQQVATARA SFYLYNTEED IDRLVAGLRS AKEYFGDVF
//
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