ID   MBHL_ALCHY              Reviewed;         621 AA.
AC   P33374;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 79.
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=hupL;
OS   Alcaligenes hydrogenophilus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1294332; DOI=10.1248/cpb.40.3292;
RA   Yagi K., Seto T., Terakado M., Umeda F., Doi T., Imanishi T., Miura Y.;
RT   "Nucleotide sequences of membrane-bound hydrogenase gene in Alcaligenes
RT   hydrogenophilus.";
RL   Chem. Pharm. Bull. 40:3292-3296(1992).
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   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; S56898; AAB25780.1; ALT_SEQ; Genomic_DNA.
DR   PIR; JH0776; JH0776.
DR   AlphaFoldDB; P33374; -.
DR   SMR; P33374; -.
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   3: Inferred from homology;
KW   Cell membrane; Membrane; Metal-binding; Nickel; Oxidoreductase.
FT   CHAIN           1..621
FT                   /note="Uptake hydrogenase large subunit"
FT                   /id="PRO_0000199707"
FT   BINDING         75
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         78
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         600
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         603
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   621 AA;  68925 MW;  906AC4414285D4A3 CRC64;
     MATYETQGFK LNDSGRRIIV DPVTRIEGHM RCEVNLDANN VIRNAVSTGT MWRGLEVILK
     RADPADAWAF VERICRVCTG CHALASVRAV EDALGIKIPK NAHLIREMMA KTLQVHDHVV
     HFYHLHALDW VDVVSALNAD PKRTSALQQT VSPAHPLSSP GYFRDVQIRL KKFVESGQLG
     PFMNGYWGNP AYKLPPEANL MAVTHYLEAL DLQKEWVKIH TIFGGKNPHP NYLVGGMPCV
     DSNLDGSGAA GAPLNMERLN FVRARIEEAI EFVKNVYLPD VLAIGTIYKD AGWLYGGGLS
     ALNVMDYGTY PRVNYDPTTD QLPGGAILNG NWDEIFPVDP RDPEQVQEFV AHSWYKYADE
     TKGLHPWDGV TEPNFVLGPK AVGTPTDIKQ LDEDAKYSWI KVAALAGHAM EVGPLVALHP
     RIRARAEDPK SYRAHYLREQ VENSARAINT GIPQALGLKQ TDYTVKQLLP TTIGRTLARA
     LEAQYCGNMM LDDWHEMMAN IKAGDLTTAN VDKWEPSAWP KEAKGVGHVA APRGACGHWI
     RIKDGKIENY QCVVPTTWNG SPRDSKGQIG AFEASLMNTP MAKPEEPVEI LRTVHSFDPC
     LACSTHVIRP DGQERVVVKV R