MBHM_ECO57
ID MBHM_ECO57 Reviewed; 567 AA.
AC P0ACE1; P37181;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
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=Z4348, ECs3879;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG58131.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37302.1; -; Genomic_DNA.
DR PIR; G85958; G85958.
DR PIR; G91113; G91113.
DR RefSeq; NP_311906.1; NC_002695.1.
DR RefSeq; WP_000083065.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0ACE1; -.
DR SMR; P0ACE1; -.
DR STRING; 155864.EDL933_4216; -.
DR PRIDE; P0ACE1; -.
DR EnsemblBacteria; AAG58131; AAG58131; Z4348.
DR EnsemblBacteria; BAB37302; BAB37302; ECs_3879.
DR GeneID; 66673108; -.
DR GeneID; 916295; -.
DR KEGG; ece:Z4348; -.
DR KEGG; ecs:ECs_3879; -.
DR PATRIC; fig|386585.9.peg.4046; -.
DR eggNOG; COG0374; Bacteria.
DR HOGENOM; CLU_030087_0_0_6; -.
DR OMA; AMFRGFE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000042990"
FT PROPEP 553..567
FT /id="PRO_0000042991"
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
