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Database: UniProt
Entry: S0EXT1_CHTCT
LinkDB: S0EXT1_CHTCT
Original site: S0EXT1_CHTCT 
ID   S0EXT1_CHTCT            Unreviewed;       386 AA.
AC   S0EXT1;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Cysteine sulfinate desulfinase/cysteine desulfurase and related enzymes {ECO:0000313|EMBL:CCW35111.1};
DE            EC=2.8.1.7 {ECO:0000313|EMBL:CCW35111.1};
GN   ORFNames=CCALI_01293 {ECO:0000313|EMBL:CCW35111.1};
OS   Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC   Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC   Chthonomonadaceae; Chthonomonas.
OX   NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW35111.1, ECO:0000313|Proteomes:UP000014227};
RN   [1] {ECO:0000313|Proteomes:UP000014227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23976 / ICMP 18418 / T49
RC   {ECO:0000313|Proteomes:UP000014227};
RA   Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA   Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT   "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT   from the Armatimonadetes phylum (formally candidate division OP10).";
RL   Submitted (MAR-2013) 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}.
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DR   EMBL; HF951689; CCW35111.1; -; Genomic_DNA.
DR   RefSeq; WP_016482652.1; NC_021487.1.
DR   AlphaFoldDB; S0EXT1; -.
DR   STRING; 454171.CP488_02802; -.
DR   KEGG; ccz:CCALI_01293; -.
DR   PATRIC; fig|1303518.3.peg.1318; -.
DR   eggNOG; COG1104; Bacteria.
DR   HOGENOM; CLU_003433_0_0_0; -.
DR   InParanoid; S0EXT1; -.
DR   OrthoDB; 9808002at2; -.
DR   Proteomes; UP000014227; Chromosome.
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:UP000014227};
KW   Transferase {ECO:0000313|EMBL:CCW35111.1}.
FT   DOMAIN          5..365
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   386 AA;  41803 MW;  C135CE1800E7B09B CRC64;
     MQLPIYLDHA ATTPVLPEVA EAMMPFLVQT YANPSAAHAL GIEARHAVEE ARGIVAEAIH
     AYPDEIVFTS GGTESDNAAI YGVAYALENR GRHILSSPIE HHAVLEPLQY LAQRGWEIEM
     LPVSSEGLVA PEEVARRIRN DTVLVSVMHA NNEIGTVQPI EAIGAICREK GVLFHTDAVQ
     SFGYLPIDVR KMNIDLLSLT AHKFYGPKGI GVLYVRSGIP FEPYQKGGGQ ENGRRGGTLN
     VPGIVGLGKA VTMVMEQREG ESARLQRLRD HFIAAVEQAI PEATLTGHRQ YRLPNNVHFC
     FKGIEGESLL LSLDAEGICA SAGAACSAGS HEPSHVLQAI GVPPDRLRGA LRLSLGRATT
     EEALEYCLHV LQKAVGALRQ KQRVQT
//
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