ID   MBHL_AZOCH              Reviewed;         601 AA.
AC   P18191; Q43952;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   10-JUN-2026, entry version 93.
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; Synonyms=hupB;
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2215219; DOI=10.1111/j.1365-2958.1990.tb00672.x;
RA   Ford C.M., Garg N., Garg R.P., Tibelius K.H., Yates M.G., Arp D.J.,
RA   Seefeldt L.C.;
RT   "The identification, characterization, sequencing and mutagenesis of the
RT   genes (hupSL) encoding the small and large subunits of the H2-uptake
RT   hydrogenase of Azotobacter chroococcum.";
RL   Mol. Microbiol. 4:999-1008(1990).
RN   [2]
RP   SEQUENCE REVISION TO 194 AND 564.
RA   Yates M.G.;
RL   Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 428-601.
RX   PubMed=7966281; DOI=10.1016/0022-2836(94)90029-9;
RA   Du L., Tibelius K.H., Souza E.M., Garg R.P., Yates M.G.;
RT   "Sequences, organization and analysis of the hupZMNOQRTV genes from the
RT   Azotobacter chroococcum hydrogenase gene cluster.";
RL   J. Mol. Biol. 243:549-557(1994).
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=H2 + A = 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; X52961; CAA37134.1; -; Genomic_DNA.
DR   EMBL; L25315; AAA64446.1; -; Genomic_DNA.
DR   PIR; S11777; S11777.
DR   PIR; S53655; S53655.
DR   AlphaFoldDB; P18191; -.
DR   SMR; P18191; -.
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   FunFam; 1.10.645.10:FF:000002; Hydrogenase 2 large subunit; 1.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   InterPro; IPR050867; NiFe/NiFeSe_hydrgnase_LSU.
DR   PANTHER; PTHR42958; HYDROGENASE-2 LARGE CHAIN; 1.
DR   PANTHER; PTHR42958:SF2; UPTAKE HYDROGENASE LARGE SUBUNIT; 1.
DR   Pfam; PF27537; HoxH; 1.
DR   Pfam; PF00374; NiFeSe_Hases; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 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..601
FT                   /note="Uptake hydrogenase large subunit"
FT                   /id="PRO_0000199708"
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         580
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   CONFLICT        444..450
FT                   /note="GLKQFLP -> ASSSSAL (in Ref. 1; CAA37134)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        457
FT                   /note="L -> S (in Ref. 1; CAA37134)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        495..498
FT                   /note="DPST -> GPEH (in Ref. 1; CAA37134)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        515..517
FT                   /note="ALG -> RSA (in Ref. 1; CAA37134)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   601 AA;  66546 MW;  568E6387C2E342FD CRC64;
     MSSLPNASQL DKSGRRIVVD PVTRIEGHMR CEVNVDANNI ITNAVSTGTM WRGLEVILKG
     RDPRDAWAFV ERICGVCTGT TRWTSVRAVE DALGIQIPYN AHLIRNLMDK QLQVQDHIVP
     FYHLLRLDWV NPVNALKADP KATSALPAAL AAHAKSSPGY FRHVQTRLKK FVESGATACS
     PNGYWDNPAY QAPARPDLMA VAHYLEALDV QKDIVEIHTI FGGKNPHPNY MVGGVACAIN
     LDDVGAAGGR STCTSLNFVL ERIHEAREFT RNVYLPDVLA VAGIYKDWLY GGGLPGHNLL
     SYGTFTKVPG DKSSDLLPAG AIVGGNWDEV LPVDVRVPEE IQEFVSHSWY RYADETKGLH
     PWDGVTEPKF ELGPNTKGTR TNIKELDEAH KYSWIKARAW RGHAMEVGPL ARYIIAYRSG
     REYVKEQVDR SLAAFNQSTG LNLGLKQFLP STLGRTLARA LECELAVDSM LDDWQALVGN
     IKAGDRATAN VEKWDPSTWP KEAKGVGINE APRGALGHWI RLKDGKIENY QAIVPTTWNG
     TPRDHLGNIG AYEAALLNTR MERPDEPVEI LRTLHSFDPC LACSTHVMSP DGQELTRVKV
     R
//