ID   MBHL_AFIC5              Reviewed;         604 AA.
AC   O33406; F8C127; Q6LB92;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Uptake hydrogenase large subunit;
DE            EC=1.12.99.6;
DE   AltName: Full=Hydrogenlyase;
DE   AltName: Full=Membrane-bound hydrogenase large subunit;
GN   Name=hoxL; OrderedLocusNames=OCA5_pHCG300630;
OS   Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS   (Oligotropha carboxidovorans).
OG   Plasmid megaplasmid pHCG3.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Afipia.
OX   NCBI_TaxID=504832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-28.
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=9324252; DOI=10.1128/jb.179.19.6053-6060.1997;
RA   Santiago B., Meyer O.;
RT   "Purification and molecular characterization of the H2 uptake membrane-
RT   bound NiFe-hydrogenase from the carboxidotrophic bacterium Oligotropha
RT   carboxidovorans.";
RL   J. Bacteriol. 179:6053-6060(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=14644498; DOI=10.1016/j.gene.2003.08.027;
RA   Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.;
RT   "Complete nucleotide sequence of the circular megaplasmid pHCG3 of
RT   Oligotropha carboxidovorans: function in the chemolithoautotrophic
RT   utilization of CO, H(2) and CO(2).";
RL   Gene 322:67-75(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=21742883; DOI=10.1128/jb.05619-11;
RA   Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA   Meyer O.;
RT   "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT   carboxidovorans strains OM4 and OM5.";
RL   J. Bacteriol. 193:5043-5043(2011).
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. {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.
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; CP002827; AEI08137.1; -; Genomic_DNA.
DR   RefSeq; WP_013913761.1; NC_015689.1.
DR   AlphaFoldDB; O33406; -.
DR   SMR; O33406; -.
DR   EnsemblBacteria; AEI08137; AEI08137; OCA5_pHCG300630.
DR   KEGG; ocg:OCA5_pHCG300630; -.
DR   PATRIC; fig|504832.7.peg.3638; -.
DR   HOGENOM; CLU_030087_0_0_5; -.
DR   OMA; EEVTHSW; -.
DR   OrthoDB; 1967820at2; -.
DR   Proteomes; UP000007730; Plasmid pHCG3.
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   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; Plasmid; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9324252"
FT   CHAIN           2..604
FT                   /note="Uptake hydrogenase large subunit"
FT                   /id="PRO_0000199714"
FT   BINDING         76
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         79
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         583
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         586
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   604 AA;  67144 MW;  F4C5271D2B241535 CRC64;
     MSVIQTPNGY KLDNSGRRVV VDPVTRIEGH MRCEVNVDSN NVIRNAVSTG TMWRGLEVIL
     KGRDPRDAWA FVERICGVCT GCHALASVRA VENALDIRIP PNAHLIREIM AKVLQWHDHV
     VHFYHLHALD WVNPVNALKA DPKATSELQQ LVGPNHPMSS PGYFRDIQNR LKRFVESGEL
     GIFKNGYWDN PAYKLSPEAD LMATAHYLEA LDIQKEIVKI HTIFGGKNPH PNFMVGGVPC
     AINMDGDLAA GAPLNMERLN FVRARIEEAY EFSKNVYIPD VIAIATFYKG WLYGGGLSAT
     NVMDYGDYAK VNYDKSTDQL KGGAILNGNW NEVFPVDAAD PEQIQEFVAH SWYKYPDEAK
     GLHPWDGVTE HNYALGPNTK GTRTDIKQLD EAAKYSWIKS PRWRGHAVEV GPLSRYILNY
     AQGNQYVIEQ VDSSLAAFNK LAGTNLTPKQ ALPSTIGRTL ARALEAHYCA AMMLDDWKEL
     IGNIKAGDSS TANVEKWDPS TWPKEAKGYG LVAAPRGANG HWIRIKDGKI ANYQCIVPTT
     WNGSPRDPAG NIGAFEASLM NTPMERPEEP VEILRTLHSF DPCLACSTHV MSEDGENLAK
     VTVR