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Database: UniProt
Entry: J2WSV2_9SPHN
LinkDB: J2WSV2_9SPHN
Original site: J2WSV2_9SPHN 
ID   J2WSV2_9SPHN            Unreviewed;       401 AA.
AC   J2WSV2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
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=PMI04_00950 {ECO:0000313|EMBL:EJK85335.1};
OS   Sphingobium sp. AP49.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK85335.1, ECO:0000313|Proteomes:UP000006480};
RN   [1] {ECO:0000313|EMBL:EJK85335.1, ECO:0000313|Proteomes:UP000006480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP49 {ECO:0000313|EMBL:EJK85335.1,
RC   ECO:0000313|Proteomes:UP000006480};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(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   -!- 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:EJK85335.1}.
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DR   EMBL; AJVL01000016; EJK85335.1; -; Genomic_DNA.
DR   RefSeq; WP_007706736.1; NZ_CP124576.1.
DR   AlphaFoldDB; J2WSV2; -.
DR   STRING; 1144307.PMI04_00950; -.
DR   PATRIC; fig|1144307.3.peg.910; -.
DR   eggNOG; COG0520; Bacteria.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000006480; 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; 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   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          21..389
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   401 AA;  42946 MW;  119A0062B370D85A CRC64;
     MTDLAQGLRL RDDFPGVGNW HYLDSAATAQ KPTAVIDAIA RAYGPDYATV HRGVYERSAN
     MTLAYEAARR KVAGFIGAAS DSEIVYVRGA TEGINLVAQC WAGTQLKAGD RILLSTLEHH
     SNIVPWQIVA EKVGAHIDVV PLTEDGRIDL DAMRAMITPQ HRMVALAHVS NVLGSVLDCR
     RAADIAHMVG AKILIDGCQA VPRLAVDVAA LDCDFYVFSA HKLYGPTGIG VLWGRKKLLD
     IMPPYQGGGS MIDKVTFEKT TYAPAPTRFE AGTPHIVGVV GLSAAIDYVQ GIGLDAIHAH
     ECAMVAKART AISQINSVRV FGPEDSAGIL SFEVEGVHPH DVGTILDETG VAIRAGHHCA
     QPLMRHLGVE ATARASFGIY SDDSDVDALV KGIERVRKIF G
//
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