ID A0A159Z3E7_9RHOB Unreviewed; 597 AA.
AC A0A159Z3E7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AKL17_1475 {ECO:0000313|EMBL:AMY68728.1};
OS Frigidibacter mobilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY68728.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY68728.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-2015) 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}.
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DR EMBL; CP012661; AMY68728.1; -; Genomic_DNA.
DR RefSeq; WP_066811893.1; NZ_CP012661.1.
DR AlphaFoldDB; A0A159Z3E7; -.
DR STRING; 1335048.AKL17_1475; -.
DR KEGG; daa:AKL17_1475; -.
DR PATRIC; fig|1335048.3.peg.1534; -.
DR OrthoDB; 9761717at2; -.
DR Proteomes; UP000076128; Chromosome.
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}.
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; 65895 MW; 4AD4E6EE5AAC1125 CRC64;
MTITTPNGFT LDTAGQRIVV DPVTRIEGHM RCEVNVDDQG IIRNAVSTGT MWRGLEVILK
GRDPRDAWAF TERICGVCTG THALTSVRAV EDALGITIPT NANSIRNIMQ LNLQIHDHIV
HFYHLHALDW VNPVNALRAD PKATSELQQK VSPNHPLSSP GYFRDVQNRL KAFVESGQLG
IFKNGYWDNP AYLLPPEADL MATTHYLEAL DLQKEIVKIH TIFGGKNPHP NWLVGGVPCP
INVHSTGAVG AINIERLNHV SSIIDKCIEF NNNVYIPDVI AIGGFYKTWL YGGGLSGKSV
LAYGDIPENP NDFSAEQLHL PRGAIINGNL NEVLDVDVRD PGQIQEFVDH SWYEYGEPGR
GLHPWDGETK PKYELGPNAK GSRTNIEQID EAAKYSWIKA PRWKGHAMEV GPLARYVVGY
AKGHEDIKNQ VEGLLGTMGL PVSALFSTLG RTAARALESE YCGRLQKHFF DKLVANIKNG
DESTANVAKW DPSTWPKEAK GVGMTEAPRG ALGHWVKIKD GRIENYQCVV PTTWNGSPRD
AAGNIGAFEA ALMNTRVERA EEPVEILRTL HSFDPCLACS THVMSPEGHE LANVKVR
//
