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Database: UniProt
Entry: R9JV85_9FIRM
LinkDB: R9JV85_9FIRM
Original site: R9JV85_9FIRM 
ID   R9JV85_9FIRM            Unreviewed;       377 AA.
AC   R9JV85;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=C808_02991 {ECO:0000313|EMBL:EOS38149.1};
OS   Lachnospiraceae bacterium M18-1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1235792 {ECO:0000313|EMBL:EOS38149.1, ECO:0000313|Proteomes:UP000014090};
RN   [1] {ECO:0000313|EMBL:EOS38149.1, ECO:0000313|Proteomes:UP000014090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M18-1 {ECO:0000313|EMBL:EOS38149.1,
RC   ECO:0000313|Proteomes:UP000014090};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium M18-1.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- 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.
CC       {ECO:0000256|ARBA:ARBA00010447}.
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:EOS38149.1}.
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DR   EMBL; ASSV01000017; EOS38149.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9JV85; -.
DR   STRING; 1235792.C808_02991; -.
DR   PATRIC; fig|1235792.3.peg.3203; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_4_9; -.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000014090; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
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; IPR010969; Cys_dSase-rel_unknwn_funct.
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; TIGR01977; am_tr_V_EF2568; 1.
DR   PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF4; ISOPENICILLIN N EPIMERASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000014090}.
FT   DOMAIN          2..367
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   377 AA;  41320 MW;  63B1A5EF62CA624A CRC64;
     MIYLDNAATT LQKPRQVAEA VAEAMCSLGN AGRGVHEATL GASRVIFDAR KRLADFFHVE
     SPKQIAFTMN STESLNTAIK GSLQSGDHVI TTELEHNSVL RPLYEMEKMG VELTMIPSDK
     KGCIDVQDFE REIRGNTRMI VCTHGSNLTG NLVDIAAVGE TARRHRVLFC VDASQTAGVF
     PIDVQEMKID ILCFTGHKSL LGPQGTGGLY VREGVKVRPL KSGGSGVQTY RKEHPPEMPT
     ALEAGTLNGH GIAGLNAAVS YIQEMGMDVI RKREQDLMKR FYDRVKEIPG IKIYGDFSEP
     ERCPIVALNL GEYDSSEVSD ELFMTYGIAT RPGAHCAPLM HRALGTVEQG AVRFSFSHYN
     TEEEIDAAAD ALRELAE
//
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