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