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CSD_HAEIN
ID   CSD_HAEIN               Reviewed;         437 AA.
AC   Q57476; O05054;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=HI_1295;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily. {ECO:0000305}.
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DR   EMBL; L42023; AAC22941.1; -; Genomic_DNA.
DR   PIR; I64114; I64114.
DR   RefSeq; NP_439446.2; NC_000907.1.
DR   AlphaFoldDB; Q57476; -.
DR   SMR; Q57476; -.
DR   STRING; 71421.HI_1295; -.
DR   EnsemblBacteria; AAC22941; AAC22941; HI_1295.
DR   KEGG; hin:HI_1295; -.
DR   PATRIC; fig|71421.8.peg.1346; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_3_6; -.
DR   OMA; PVCLRYG; -.
DR   PhylomeDB; Q57476; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   CDD; cd06453; SufS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
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   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..437
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150298"
FT   MOD_RES         258
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   437 AA;  49048 MW;  1126FEC23DE8BB9B CRC64;
     MIRFIFKHKK MHKPKELVFG QTIIQLNQVN GADKRKLIWL LIIKRSRQAF PYFQREDAVI
     YLDNAATTLK PQVLIDRTAE FYASAGSVHR SQYDAAQTVQ YEQARTQVKE WVHAEDKHAV
     IWTSGTTHAI NLVANGLMPQ LNAEDEILIS QADHHANFVT WHETAKKCGA KIQVLPILDN
     WLIDENALIS ALSEKTKLVA LNFVSNVTGT EQPIKRLIQL IRKHSNALVL VDAAQAISHI
     KIDLQDLDAD FLAFSAHKIY GPNGLGVLTG KLTALSQLQP LFFGGKMVDR VSNDRITFAE
     LPYRLEAGTP NIAGVIGFNA VLDWLQKWDF TAAEQYAISL AESVKVRLKS YENCRLFNSP
     QASTVVCFVF DGIDCSDLST LLSEQNIALR VGEHCAQPYL ARLGERTTLR LSFAPYNTQE
     DVEAFFTALD KALDLLQ
 
 
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