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Database: UniProt
Entry: R8AQ25_PLESH
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Original site: R8AQ25_PLESH 
ID   R8AQ25_PLESH            Unreviewed;       567 AA.
AC   R8AQ25;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=hydrogenase (acceptor) {ECO:0000256|ARBA:ARBA00012082};
DE            EC=1.12.99.6 {ECO:0000256|ARBA:ARBA00012082};
GN   ORFNames=PLESHI_10455 {ECO:0000313|EMBL:EON88432.1};
OS   Plesiomonas shigelloides 302-73.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Plesiomonas.
OX   NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON88432.1, ECO:0000313|Proteomes:UP000014012};
RN   [1] {ECO:0000313|EMBL:EON88432.1, ECO:0000313|Proteomes:UP000014012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=302-73 {ECO:0000313|EMBL:EON88432.1,
RC   ECO:0000313|Proteomes:UP000014012};
RX   PubMed=23814109;
RA   Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT   "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL   Genome Announc. 1:e00404-13(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000386};
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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
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:EON88432.1}.
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DR   EMBL; AQQO01000340; EON88432.1; -; Genomic_DNA.
DR   RefSeq; WP_010863700.1; NZ_KB944511.1.
DR   AlphaFoldDB; R8AQ25; -.
DR   STRING; 703.SAMEA2665130_01611; -.
DR   PATRIC; fig|1315976.3.peg.1962; -.
DR   HOGENOM; CLU_030087_0_0_6; -.
DR   OrthoDB; 9761717at2; -.
DR   Proteomes; UP000014012; 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:0033748; F:hydrogenase (acceptor) activity; IEA:UniProtKB-EC.
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:SF1; HYDROGENASE-2 LARGE CHAIN; 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:UP000014012}.
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         61
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         64
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         64
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         546
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         549
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         552
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   567 AA;  62743 MW;  7222FE99B68090D9 CRC64;
     MSQRITIDPV TRIEGHLRID CEIANGKVVK AWSSGTMWRG MEEIVQGRDP RDAWMIMQRI
     CGVCTNIHAI GSVRAVESAL NLNVPVNAQY IRNIILAASN IHDHVVHFYQ LSALDWVDIT
     SALQADPVKA SQMLNGVSSW QLNSPQELTK VQNKIRALVD SGQLGIFANG YWGHPTMKLP
     PEVNLIAVAH YMQALEYQRD ASRVVALLGG KSPHIQNLAV GGVANPINLD GIGVLNMERL
     MYLKTFIDRL NGFIEQVYMP DAAIIASFYP EWLQSGRGVT NYLSVPELPT DNQGGSFLLQ
     GGYIKNGDMS TFRAIDSHKD QFLIDGIAES SKHAWYRDNE PLHPWQGKTR PNYTGWNEDG
     KYSWVKAPTF YGETVEVGPL ANVLCMLAAG HEGTKQHMDT VLGLYQKLSG NTLTPQEMPS
     TMGRVLARAV RCAVMKDTLA HQWQALIDNI GRGDYVAYIK PNIPADTELR GVGFEEAPRG
     MLSHWIVIKN GKIANYQAVV PSTWNSGPRN QNDEPGPYEA ALVGTPVADP EKPLEVVRTV
     HSFDPCMSCA VHIVDTRGQQ VTEVKVL
//
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