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MBHM_SHIFL
ID   MBHM_SHIFL              Reviewed;         567 AA.
AC   P0ACE2; P37181;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Hydrogenase-2 large chain;
DE            Short=HYD2;
DE            EC=1.12.99.6;
DE   AltName: Full=Membrane-bound hydrogenase 2 large subunit;
DE   AltName: Full=NiFe hydrogenase;
DE   Flags: Precursor;
GN   Name=hybC; OrderedLocusNames=SF3041, S3242;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: This is one of three E.coli hydrogenases synthesized in
CC       response to different physiological conditions. HYD2 is involved in
CC       hydrogen uptake (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6;
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250};
CC       Note=Binds 1 nickel ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN44519.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18330.1; -; Genomic_DNA.
DR   RefSeq; NP_708812.1; NC_004337.2.
DR   RefSeq; WP_000083065.1; NZ_WPGW01000034.1.
DR   AlphaFoldDB; P0ACE2; -.
DR   SMR; P0ACE2; -.
DR   STRING; 198214.SF3041; -.
DR   EnsemblBacteria; AAN44519; AAN44519; SF3041.
DR   EnsemblBacteria; AAP18330; AAP18330; S3242.
DR   GeneID; 1026601; -.
DR   GeneID; 66673108; -.
DR   KEGG; sfl:SF3041; -.
DR   KEGG; sfx:S3242; -.
DR   PATRIC; fig|198214.7.peg.3615; -.
DR   HOGENOM; CLU_030087_0_0_6; -.
DR   OMA; AMFRGFE; -.
DR   OrthoDB; 1967820at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:UniProt.
DR   Gene3D; 1.10.645.10; -; 1.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   Pfam; PF00374; NiFeSe_Hases; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR   PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Metal-binding; Nickel; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..552
FT                   /note="Hydrogenase-2 large chain"
FT                   /id="PRO_0000042992"
FT   PROPEP          553..567
FT                   /id="PRO_0000042993"
FT   BINDING         61
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         64
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         546
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         549
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   SITE            552..553
FT                   /note="Cleavage; by HybD"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   567 AA;  62491 MW;  A19E6F513390F29E CRC64;
     MSQRITIDPV TRIEGHLRID CEIENGVVSK AWASGTMWRG MEEIVKNRDP RDAWMIVQRI
     CGVCTTTHAL SSVRAAESAL NIDVPVNAQY IRNIILAAHT THDHIVHFYQ LSALDWVDIT
     SALQADPTKA SEMLKGVSTW HLNSPEEFTK VQNKIKDLVA SGQLGIFANG YWGHPAMKLP
     PEVNLIAVAH YLQALECQRD ANRVVALLGG KTPHIQNLAV GGVANPINLD GLGVLNLERL
     MYIKSFIDKL SDFVEQVYKV DTAVIAAFYP EWLTRGKGAV NYLSVPEFPT DSKNGSFLFP
     GGYIENADLS SYRPITSHSD EYLIKGIQES AKHSWYKDEA PQAPWEGTTI PAYDGWSDDG
     KYSWVKSPTF YGKTVEVGPL ANMLVKLAAG RESTQNKLNE IVAIYQKLTG NTLEVAQLHS
     TLGRIIGRTV HCCELQDILQ NQYSALITNI GKGDHTTFVK PNIPATGEFK GVGFLEAPRG
     MLSHWMVIKD GIISNYQAVV PSTWNSGPRN FNDDVGPYEQ SLVGTPVADP NKPLEVVRTI
     HSFDPCMACA VHVVDADGNE VVSVKVL
 
 
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