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Database: UniProt
Entry: J9DXP6_9PROT
LinkDB: J9DXP6_9PROT
Original site: J9DXP6_9PROT 
ID   J9DXP6_9PROT            Unreviewed;       413 AA.
AC   J9DXP6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558, ECO:0000256|RuleBase:RU004506};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN   ORFNames=IMCC14465_02060 {ECO:0000313|EMBL:EJW21812.1};
OS   alpha proteobacterium IMCC14465.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; PS1 clade.
OX   NCBI_TaxID=1220535 {ECO:0000313|EMBL:EJW21812.1, ECO:0000313|Proteomes:UP000004836};
RN   [1] {ECO:0000313|EMBL:EJW21812.1, ECO:0000313|Proteomes:UP000004836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC14465 {ECO:0000313|EMBL:EJW21812.1,
RC   ECO:0000313|Proteomes:UP000004836};
RX   PubMed=23209213; DOI=10.1128/JB.01888-12;
RA   Yang S.J., Kang I., Cho J.C.;
RT   "Genome Sequence of Strain IMCC14465, Isolated from the East Sea, Belonging
RT   to the PS1 Clade of Alphaproteobacteria.";
RL   J. Bacteriol. 194:6952-6953(2012).
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   -!- FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine
CC       to produce alanine. Seems to participate in the biosynthesis of the
CC       nitrogenase metalloclusters by providing the inorganic sulfur required
CC       for the Fe-S core formation. {ECO:0000256|ARBA:ARBA00003120}.
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:EJW21812.1}.
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DR   EMBL; ALYF01000002; EJW21812.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9DXP6; -.
DR   STRING; 1220535.IMCC14465_02060; -.
DR   PATRIC; fig|1220535.3.peg.204; -.
DR   eggNOG; COG0520; Bacteria.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000004836; 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:SF8; 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:UP000004836};
KW   Transferase {ECO:0000256|RuleBase:RU004506}.
FT   DOMAIN          32..401
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   413 AA;  45547 MW;  2A49FB1050648B62 CRC64;
     MTISAASAAY NVDKVRADFP ILSMEVYGKP LIYLDNAASA QKPLQVMNAM NEAMTSGYAN
     VHRGLHYLSN KATDDFEVAR EDVRRFLNAP SLEEVIFTGG ATDALNLVAQ CYGADHIGEG
     DEIILSEMEH HSNIVPWHYL REHKGAVIKW VRVHDDGSFD MEDYKNLLGP KTKFVALTQM
     SNALGTITPM KEIIRLAHAY DAPVLVDGCQ GAVHLETDVQ DLDCDFYVLS GHKLYGPSGI
     GALYGKAEYL NKMRPYRGGG EMIREVTLDN VTYGDLPHKF EAGTPPILEV IGLGAALRYI
     ESYGRKEIAA HEHDLLEYAT RKMTEINNLT IMGTAPEKGS VISFTIKDIH PHDLATVVDR
     SGVAVRAGHH CAQPLMNRFG VTATARASFA MYNTRDEIDS LVESIHKAIS FFG
//
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