MBHL_WOLSU
ID MBHL_WOLSU Reviewed; 576 AA.
AC P31883;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Quinone-reactive Ni/Fe-hydrogenase large chain;
DE EC=1.12.5.1;
DE AltName: Full=Hydrogen:quinone oxidoreductase;
DE AltName: Full=Membrane-bound hydrogenase large subunit;
GN Name=hydB; OrderedLocusNames=WS1686;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RX PubMed=1587288; DOI=10.1111/j.1432-1033.1992.tb16905.x;
RA Dross F., Geisler V., Lenger R., Theis F., Krafft T., Fahrenholz F.,
RA Kojro E., Duchene A., Tripier D., Juvenal K., Kroeger A.;
RT "The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes.";
RL Eur. J. Biochem. 206:93-102(1992).
RN [2]
RP ERRATUM OF PUBMED:1587288.
RX PubMed=8319698;
RA Dross F., Geisler V., Lenger R., Theis F., Krafft T., Fahrenholz F.,
RA Kojro E., Duchene A., Tripier D., Juvenal K., Kroeger A.;
RL Eur. J. Biochem. 214:949-950(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
CC -!- FUNCTION: This enzyme recycles the H(2) produced by nitrogenase to
CC increase the production of ATP and to protect nitrogenase against
CC inhibition or damage by O(2) under carbon- or phosphate-limited
CC conditions.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a menaquinone + H2 = a menaquinol; Xref=Rhea:RHEA:18641,
CC Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539, ChEBI:CHEBI:16374,
CC ChEBI:CHEBI:18151, ChEBI:CHEBI:18276; EC=1.12.5.1;
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.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000305}.
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DR EMBL; X65189; CAA46303.1; -; Genomic_DNA.
DR EMBL; BX571661; CAE10713.1; -; Genomic_DNA.
DR PIR; S33853; S33853.
DR RefSeq; WP_011139497.1; NC_005090.1.
DR AlphaFoldDB; P31883; -.
DR SMR; P31883; -.
DR STRING; 273121.WS1686; -.
DR TCDB; 3.D.7.2.2; the h2:heterodisulfide oxidoreductase (hho) family.
DR EnsemblBacteria; CAE10713; CAE10713; WS1686.
DR KEGG; wsu:WS1686; -.
DR eggNOG; COG0374; Bacteria.
DR HOGENOM; CLU_030087_0_0_7; -.
DR OMA; CTHIHAL; -.
DR OrthoDB; 1967820at2; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0047067; F:hydrogen:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Membrane; Metal-binding; Nickel;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1587288"
FT CHAIN 2..576
FT /note="Quinone-reactive Ni/Fe-hydrogenase large chain"
FT /id="PRO_0000199718"
FT BINDING 62
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 65
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 547
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 550
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
SQ SEQUENCE 576 AA; 63977 MW; 091357213B6FF84E CRC64;
MTKRIVVDPI TRIEGHLRIE VVVDENNVIQ DAFSTATLWR GLETILKGRD PRDAGFFTQR
ICGVCTYSHY KAGISAVENA LGIKPPLNAE LIRSLMSISL ILHDHTVHFY HLHGLDWCDI
TSALKADPVA ASKLAFKYSP NPIATGADEL TAVQKRVAEF AAKGNLGPFA NAYWGHKTYR
FSPEQNLIVL SHYLKALEVQ RVAAQMMAIW GAKQPHPQSL TVGGVTSVMD ALDPSRLGDW
LTKYKYVADF VNRAYYADVV MAAEVFKSEP SVLGGCNVKN FYSYQEIPLN KTEWMYSTGI
VMDGDITKVH EINEDLITEE ATHAWYKENK ALHPYDGQQD PNYTGFKDME TVGPDGTMVK
TKVIDEKGKY TWIKAPRYGG KPLEVGPLAT IVVGLAAKNP RIEKVATQFL KDTGLPLAAL
FTTLGRTAAR MLECKLSADY GFEAFNSLIA NLKVDQSTYT TYKIDKNKEY KGRYMGTVPR
GVLSHWVRIK NGVIQNYQAV VPSTWNAGPR DANGTKGPYE ASLVGMKLQD LSQPLEIIRV
IHSFDPCIAC AVHVMDTKGN ELSQYRVDPI TVGCNL
