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Database: UniProt
Entry: J5WBC2_9FIRM
LinkDB: J5WBC2_9FIRM
Original site: J5WBC2_9FIRM 
ID   J5WBC2_9FIRM            Unreviewed;       397 AA.
AC   J5WBC2;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:EJU20707.1};
DE            EC=2.8.1.7 {ECO:0000313|EMBL:EJU20707.1};
GN   Name=iscS {ECO:0000313|EMBL:EJU20707.1};
GN   ORFNames=HMPREF1152_0771 {ECO:0000313|EMBL:EJU20707.1};
OS   Mogibacterium sp. CM50.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis; Mogibacterium.
OX   NCBI_TaxID=936375 {ECO:0000313|EMBL:EJU20707.1, ECO:0000313|Proteomes:UP000003142};
RN   [1] {ECO:0000313|EMBL:EJU20707.1, ECO:0000313|Proteomes:UP000003142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM50 {ECO:0000313|EMBL:EJU20707.1,
RC   ECO:0000313|Proteomes:UP000003142};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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. NifS/IscS subfamily.
CC       {ECO:0000256|ARBA:ARBA00006490}.
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:EJU20707.1}.
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DR   EMBL; ALNL01000035; EJU20707.1; -; Genomic_DNA.
DR   RefSeq; WP_009644135.1; NZ_ALNL01000035.1.
DR   AlphaFoldDB; J5WBC2; -.
DR   STRING; 936375.HMPREF1152_0771; -.
DR   PATRIC; fig|936375.3.peg.1033; -.
DR   eggNOG; COG1104; Bacteria.
DR   OrthoDB; 9808002at2; -.
DR   Proteomes; UP000003142; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.260.50; -; 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; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003142};
KW   Transferase {ECO:0000313|EMBL:EJU20707.1}.
FT   DOMAIN          3..365
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   397 AA;  43191 MW;  3B9AE1619040744E CRC64;
     MKVYADNAAT TYLNDVALNT LLDCLKNYNG NPNSLHTDGQ VAQEKLDESR AKVAEAINAA
     KPNEIYFTSG GSEADNQALI SAARGLVKKG KKHLISLNIE HHAILHTLAK LEKEGFEVTL
     LKPQPNGIVD VKDVENAIRE DTALVSIMFA NNEMGAIQPI AEIGKLCHDK RVLFHTDAVQ
     AVAHLPIDVQ AMNIDMLSMS AHKFHGPKGV GALYARNGIR LINVIEGGAQ ERGKRAGTVN
     VPGNAALAAA LEDGVLHMEE NARKTAALRD RLIKGLSDIP YSQLNGDPVK RLPGNVNYSF
     EGVEGESLLL ALDMYGIECS SGSACTSESL DPSHVLVGMG VPVEAAHGSL RFSLNEENTE
     EQVDYIIEKV HEVVEHYRKL SPFWDELEKG EREHVIQ
//
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