ID   MBHL_AZOVI              Reviewed;         602 AA.
AC   P21949;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Uptake hydrogenase large subunit;
DE            EC=1.12.99.6;
DE   AltName: Full=Hydrogenase subunit alpha;
DE   AltName: Full=Hydrogenlyase;
DE   AltName: Full=Membrane-bound hydrogenase large subunit;
GN   Name=hoxG;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=2265761; DOI=10.1016/0378-1119(90)90342-o;
RA   Menon A.L., Stults L.W., Robson R.L., Mortenson L.E.;
RT   "Cloning, sequencing and characterization of the [NiFe]hydrogenase-encoding
RT   structural genes (hoxK and hoxG) from Azotobacter vinelandii.";
RL   Gene 96:67-74(1990).
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 + 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   -!- PTM: 15 or 16 residues are removed from the C-terminus during
CC       maturation of the protein.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; M33152; AAA82506.1; -; Genomic_DNA.
DR   EMBL; L23970; AAA19499.1; -; Unassigned_DNA.
DR   PIR; JQ0806; JQ0806.
DR   RefSeq; WP_012703499.1; NZ_FPKM01000029.1.
DR   AlphaFoldDB; P21949; -.
DR   SMR; P21949; -.
DR   OMA; EEVTHSW; -.
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.
FT   CHAIN           1..602
FT                   /note="Uptake hydrogenase large subunit"
FT                   /id="PRO_0000199709"
FT   BINDING         74
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         77
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         581
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         584
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   602 AA;  66737 MW;  BCC64BB2F12B3240 CRC64;
     MSSLPNASQL DKSGRRIVVD PVTRIEGHMR CEVNVDASNV ITNAVSTGTM WRGLEVILKG
     RDPRDAWAFV ERICGVCTGT HALTSVRAVE DALDIRIPYN AHLIRNLMDK TLQVHDHIVH
     FYHLHALDWV NPVNALKADP KATSALQQAV SPAHAKSSPG YFRDVQTRLK KFVESGQLGL
     FSNGYWDNPA YKLPPEADLM AVAHYLEALD LQKDIVKIHT IFGGKNPHPN YMVGGVACAI
     NLDDVGAAGA PVNMTSLNFV LERIHEAREF TRNVYLPDVL AVAGIYKDWL YGGGLAAHNL
     LSYGTFTKVP YDKSSDLLPA GAIVGGNWDE VLPVDVRDPE EIQEFVSHSW YSYADETKGL
     HPWDGVTEPK FELGPNTKGS RTHIQEIDEA HKYSWIKAPR WRGHAMEVGP LARYIIAYAS
     GREYVKEQVD RSLAAFNQST GLNLGLKQFL PSTLGRTLAR ALECELAVDS MLDDWQALVG
     NIKAGDRATA NVEKWDPSTW PKEAKGVGIN EAPRGALGHW IRIKDGKIEN YQAIVPTTWN
     GTPRDHLGNI GAYEAALLNT RMERPDEPVE ILRTLHSFDP CLACSTHVMS PDGQELTRVK
     VR