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Entry: A0A317ED54_9PROT
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ID   A0A317ED54_9PROT        Unreviewed;       604 AA.
AC   A0A317ED54;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=DKG75_00820 {ECO:0000313|EMBL:PWR23145.1};
OS   Zavarzinia compransoris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Zavarziniaceae; Zavarzinia.
OX   NCBI_TaxID=1264899 {ECO:0000313|EMBL:PWR23145.1, ECO:0000313|Proteomes:UP000246077};
RN   [1] {ECO:0000313|Proteomes:UP000246077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1231 {ECO:0000313|Proteomes:UP000246077};
RA   Lee Y., Jeon C.O.;
RT   "Zavarzinia sp. HR-AS.";
RL   Submitted (MAY-2018) 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:PWR23145.1}.
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DR   EMBL; QGLF01000001; PWR23145.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317ED54; -.
DR   OrthoDB; 9761717at2; -.
DR   Proteomes; UP000246077; 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:UP000246077}.
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         76
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         79
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         79
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         583
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         586
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         589
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   604 AA;  67124 MW;  2F0EAFC87DA33E32 CRC64;
     MGIIQTPNGF SLDNTGKRVV VDPVTRIEGH MRCEVNLDSN NVIRNAVSTG TMWRGLEVIL
     KGRDPRDAWA FVERICGVCT GCHALTSVRA VEDALGITIP KNAHLIREMM AKTLQWHDHV
     VHFYHLHALD WVNPVNALKA DPKATSELQQ MVSPSHPMSS PGYFRDIQNR LKKFVESGQL
     GIFKNGYWDN PAYKLPPEAD LMAVTHYLEA LDLQKEVVKI HTIFGGKNPH PNFMVGGVPC
     AINMEGNMSA GAPLNMERLN FVRARIQEAY DFSKNVYIPD VIAIASFYKN WLYGGGLSAT
     NVLDYGDYES VLGDKSTDRL PGGVILNGNW NEIHPIDPRD PTQVQEFVTH SWYTYGDDSK
     GLHPWDGITQ PKYELGPNAK GTRTNIKELD ESAKYSWIKS PRWKGHACEV GPLARYILAY
     AHGVTYVKDQ VHDSLGRFNA LAGTSLTPQQ ALPSTIGRTL ARALEAHYCA EMMLNDWDEL
     IANIKAGDLA TANVEKWDPK TWPSEAKGVG TVAAPRGGLG HWIRIKDGRI ENYQCVVPTT
     WNGSPRDPAG NIGAFEASLM NTPMERPEEP VEILRTLHSF DPCLACSTHV MAPDGEELAR
     VQVR
//
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