(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIT9_GEOS0

ID   A0A0F6BIT9_GEOS0        Unreviewed;       406 AA.
AC   A0A0F6BIT9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 34.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|RuleBase:RU004506, ECO:0000256|SAAS:SAAS00062216};
DE            EC=2.8.1.7 {ECO:0000256|RuleBase:RU004506, ECO:0000256|SAAS:SAAS00062216};
GN   OrderedLocusNames=GY4MC1_0508 {ECO:0000313|EMBL:ADP73340.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73340.1};
RN   [1] {ECO:0000313|EMBL:ADP73340.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73340.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004506,
CC         ECO:0000256|SAAS:SAAS01122505};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU004504,
CC         ECO:0000256|SAAS:SAAS00608357};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily. {ECO:0000256|RuleBase:RU004506,
CC       ECO:0000256|SAAS:SAAS00544087}.
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DR   EMBL; CP002293; ADP73340.1; -; Genomic_DNA.
DR   RefSeq; WP_013400068.1; NC_014650.1.
DR   SMR; A0A0F6BIT9; -.
DR   EnsemblBacteria; ADP73340; ADP73340; GY4MC1_0508.
DR   GeneID; 29236840; -.
DR   KEGG; gmc:GY4MC1_0508; -.
DR   KO; K11717; -.
DR   OMA; HKLCGPT; -.
DR   OrthoDB; 446447at2; -.
DR   BioCyc; GSP581103:G1GOQ-559-MONOMER; -.
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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIT9.
DR   SWISS-2DPAGE; A0A0F6BIT9.
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004506,
KW   ECO:0000256|SAAS:SAAS00427524};
KW   Transferase {ECO:0000256|RuleBase:RU004506, ECO:0000256|SAAS:SAAS00062250}.
FT   DOMAIN          23..391
FT                   /note="Aminotran_5"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   406 AA;  44929 MW;  0F688A25070B7BA6 CRC64;
     MNTKEIRRLF PILDQKVNGK PLVYLDNAAT SQKPLSVIET LDRYYREYNS NVHRGVHTLG
     TKATDAYEGA REKVRRFINA KSTQEIIFTR GTTAALNMVA TSYGRANLQE GDEIVITYME
     HHSNLIPWQQ AAKQTGATLK YIPLQADGTI DMKDVEATVT ENTKIVAIAH VSNVLGTINP
     IKEIARVAHQ RGAVIVVDAA QSAPHMKIDV QDLDCDFLAF SGHKMCGPTG IGVLYGKREL
     LEKMEPVEFG GEMIDFVDLY ESTWKELPWK FEGGTPIIAG AVGLGAAIDF LEDIGLDHIA
     AHEQELAQYA LERLSAIKGL AIYGPKHRGG LVTFNIEGVH PHDVATVLDA EGIAIRAGHH
     CAQPLMKWLN VTATARASFY LYNTKEEIDQ FVDALQKAKE YFGHVF
//

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