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Database: UniProt
Entry: A0A1B9YGV8_9BRAD
LinkDB: A0A1B9YGV8_9BRAD
Original site: A0A1B9YGV8_9BRAD 
ID   A0A1B9YGV8_9BRAD        Unreviewed;       596 AA.
AC   A0A1B9YGV8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Uptake hydrogenase large subunit {ECO:0000256|ARBA:ARBA00040803};
DE   AltName: Full=Hydrogenlyase {ECO:0000256|ARBA:ARBA00042683};
DE   AltName: Full=Membrane-bound hydrogenase large subunit {ECO:0000256|ARBA:ARBA00041237};
GN   ORFNames=LMTR3_22505 {ECO:0000313|EMBL:OCK53960.1};
OS   Bradyrhizobium sp. LMTR 3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=189873 {ECO:0000313|EMBL:OCK53960.1, ECO:0000313|Proteomes:UP000093220};
RN   [1] {ECO:0000313|EMBL:OCK53960.1, ECO:0000313|Proteomes:UP000093220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMTR 3 {ECO:0000313|EMBL:OCK53960.1,
RC   ECO:0000313|Proteomes:UP000093220};
RA   Ormeno-Orrillo E., Duran D., Rey L., Ruiz Argueso T., Imperial J.,
RA   Martinez E.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00037655}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000256|ARBA:ARBA00001967,
CC         ECO:0000256|PIRSR:PIRSR601501-1};
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC       {ECO:0000256|ARBA:ARBA00011771}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000256|ARBA:ARBA00009292, ECO:0000256|RuleBase:RU003896}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OCK53960.1}.
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DR   EMBL; MAXC01000053; OCK53960.1; -; Genomic_DNA.
DR   RefSeq; WP_065749144.1; NZ_MAXC01000053.1.
DR   AlphaFoldDB; A0A1B9YGV8; -.
DR   STRING; 189873.LMTR3_22505; -.
DR   OrthoDB; 9761717at2; -.
DR   Proteomes; UP000093220; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
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   PANTHER; PTHR42958; HYDROGENASE-2 LARGE CHAIN; 1.
DR   PANTHER; PTHR42958:SF2; UPTAKE HYDROGENASE LARGE SUBUNIT; 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   Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601501-1};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRSR:PIRSR601501-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003896};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093220}.
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         75
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         78
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         78
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         575
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         578
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         581
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   596 AA;  66081 MW;  565BA16268EAA1B1 CRC64;
     MGAQTPNGFK LDNSSKRIVV DPLTRVEGHL RVEVNLDSDN VICNAVSSGT MWRGIETILR
     GRDPRDAWAF TERICGVCTG THALTSVRAV ENALGISIPE NANSIRNIMQ LCLQVHDHLV
     HFYHLHSLDW VDVISALKAD PKATSALAQS VSPWPLSSPG YFKHLQIRLT KFVESGQLGP
     FKNAYWGHPA YKLPPEANLM ALAHYLEALD FQKDVVKIHA IYGGKNPHPN WLVGGVACAI
     NVDGTGAVGA INMERLNLVS SIIGRSIEFV EQVYLPDVTV IGCFYKDWLY GCGLSGKSVM
     SYGDIPENAN DYSAKNLKQP RGVILNGNFS EVLPIDHGDP EQIQEFVAHS WYKYPDERRG
     LHPWDGITEP NFRLGPNVKG TTTDIKELDE GGKYSWIKAP RWRGNAVEVG PLARYLIGHA
     QGKEEFKEPT EKLLKTLDLP FAALFSTLGR TAARALECQW AAHQMRYFQD KLMAHIKAGD
     TATANVDKWK PESWPKEAKG YGFTEAPRGA LGHWIKIKET KIDNYQCVVP TTWNGSPRDP
     NGNIGAFEAS LMDTPIADPE KPLEILRTIH SFDPCLACST HVMGPDGQEM ATIKVR
//
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