ID A0A2T7UL47_9RHOB Unreviewed; 597 AA.
AC A0A2T7UL47;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=DDE23_21645 {ECO:0000313|EMBL:PVE45397.1};
OS Pararhodobacter aggregans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pararhodobacter.
OX NCBI_TaxID=404875 {ECO:0000313|EMBL:PVE45397.1, ECO:0000313|Proteomes:UP000244810};
RN [1] {ECO:0000313|EMBL:PVE45397.1, ECO:0000313|Proteomes:UP000244810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-19 {ECO:0000313|EMBL:PVE45397.1,
RC ECO:0000313|Proteomes:UP000244810};
RX PubMed=21959289; DOI=10.1016/j.syapm.2011.08.006;
RA Foesel B.U., Drake H.L., Schramm A.;
RT "Defluviimonas denitrificans gen. nov., sp. nov., and Pararhodobacter
RT aggregans gen. nov., sp. nov., non-phototrophic Rhodobacteraceae from the
RT biofilter of a marine aquaculture.";
RL Syst. Appl. Microbiol. 34:498-502(2011).
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:PVE45397.1}.
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DR EMBL; QDDR01000015; PVE45397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7UL47; -.
DR OrthoDB; 9761717at2; -.
DR Proteomes; UP000244810; 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:UP000244810}.
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 576
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 579
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 582
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 597 AA; 66448 MW; 7218F7DC01F7F9A6 CRC64;
MVIQTPNGFS LDNSGRRIVV DPVTRIEGHM RCEVNVDENG VIRNAVSTGT MWRGLEVILR
GRDPRDAWAF TERICGVCTG THALTSVRAV EDALGITIPE NANSIRNMMQ LNLEIHDHVV
HFYHLHALDW VNPINALRAD PRATSELQQA VSPSHPMSSP GYFRDVQARL RAFVESGQLG
LFKNGYWDNP AYKLPPEADL MATVHYLEAL DLQKEIVKVH TIFGGKNPHP NWLVGGVPCP
INMHSTGAVG AINMERLNLV SSIIQKCTDF VNNVYIPDVV AIGGFYKTWL YGGGLSSKAC
LAYGDIPEHP NNFDPAQLYL PRGAIINGNL NEVHEVDVRD PEQIQEFVDH SWYEYGQPGQ
GKHPWDGETS PRYELGPNAR GTRTNIEELD EAAKYSWIKA PRWRGHAMEV GPLARYIVGY
AQGHEDITNQ INGLLRTMDL PVEALFSTLG RTAARALEAE YCARLQRHFF DKLVANIRNG
DQSTANVAKW DPSTWPREAR GVGMTEAPRG ALGHWISIKD GKIENYQCVV PTTWNGSPRD
AQGNIGAFEA SLMDTPMERP DEPVEILRTL HSFDPCLACS THVMSPDGQE LTSVKVR
//
