MBHL_CUPNH
ID MBHL_CUPNH Reviewed; 618 AA.
AC P31891; Q7WXU5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Uptake hydrogenase large subunit;
DE EC=1.12.99.6;
DE AltName: Full=Hydrogenlyase;
DE AltName: Full=Membrane-bound hydrogenase large subunit;
GN Name=hoxG; OrderedLocusNames=PHG002;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1383192; DOI=10.1128/jb.174.19.6277-6289.1992;
RA Kortlueke C., Horstmann K., Schwartz E., Rohde M., Binsack R.,
RA Friedrich B.;
RT "A gene complex coding for the membrane-bound hydrogenase of Alcaligenes
RT eutrophus H16.";
RL J. Bacteriol. 174:6277-6289(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
RN [3]
RP PROTEIN SEQUENCE OF 2-31.
RX PubMed=2493816; DOI=10.1016/0167-4838(89)90225-2;
RA Lorenz B., Schneider K., Kratzin H., Schlegel H.G.;
RT "Immunological comparison of subunits isolated from various hydrogenases of
RT aerobic hydrogen bacteria.";
RL Biochim. Biophys. Acta 995:1-9(1989).
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.
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 -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250};
CC Note=Binds 1 nickel ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC -!- INTERACTION:
CC P31891; P31892: hoxK; NbExp=3; IntAct=EBI-15948409, EBI-15948434;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000305}.
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DR EMBL; M96433; AAA16462.1; -; Unassigned_DNA.
DR EMBL; AY305378; AAP85758.1; -; Genomic_DNA.
DR PIR; B43255; B43255.
DR RefSeq; WP_011153927.1; NZ_CP039289.1.
DR PDB; 3RGW; X-ray; 1.50 A; L=1-603.
DR PDB; 4IUB; X-ray; 1.61 A; L=1-603.
DR PDB; 4IUC; X-ray; 1.45 A; L=1-603.
DR PDB; 4IUD; X-ray; 1.45 A; L=1-603.
DR PDB; 4TTT; X-ray; 1.72 A; L=1-603.
DR PDB; 5D51; X-ray; 1.47 A; L=1-603.
DR PDB; 5MDJ; X-ray; 1.48 A; L=1-603.
DR PDB; 5MDK; X-ray; 1.50 A; L=1-603.
DR PDB; 5MDL; X-ray; 1.41 A; L=1-603.
DR PDB; 7ODG; X-ray; 1.62 A; L=1-603.
DR PDB; 7ODH; X-ray; 1.34 A; L=1-603.
DR PDBsum; 3RGW; -.
DR PDBsum; 4IUB; -.
DR PDBsum; 4IUC; -.
DR PDBsum; 4IUD; -.
DR PDBsum; 4TTT; -.
DR PDBsum; 5D51; -.
DR PDBsum; 5MDJ; -.
DR PDBsum; 5MDK; -.
DR PDBsum; 5MDL; -.
DR PDBsum; 7ODG; -.
DR PDBsum; 7ODH; -.
DR AlphaFoldDB; P31891; -.
DR SMR; P31891; -.
DR DIP; DIP-59144N; -.
DR IntAct; P31891; 1.
DR STRING; 381666.PHG002; -.
DR EnsemblBacteria; AAP85758; AAP85758; PHG002.
DR GeneID; 39976548; -.
DR KEGG; reh:PHG002; -.
DR PATRIC; fig|381666.6.peg.2; -.
DR eggNOG; COG0374; Bacteria.
DR HOGENOM; CLU_030087_0_0_4; -.
DR OMA; EEVTHSW; -.
DR OrthoDB; 1967820at2; -.
DR BioCyc; MetaCyc:HOXGALCA-MON; -.
DR BRENDA; 1.12.99.6; 231.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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; -; 1.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR InterPro; IPR029014; NiFe-Hase_large.
DR Pfam; PF00374; NiFeSe_Hases; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Membrane;
KW Metal-binding; Nickel; Oxidoreductase; Plasmid; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2493816"
FT CHAIN 2..618
FT /note="Uptake hydrogenase large subunit"
FT /id="PRO_0000199706"
FT BINDING 75
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 78
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 597
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 600
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT CONFLICT 578
FT /note="M -> V (in Ref. 1; AAA16462)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:7ODH"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 100..124
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 196..216
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:3RGW"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:5MDL"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 255..274
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:7ODH"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 413..425
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 432..446
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 448..453
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 469..499
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 518..528
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 531..540
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 543..550
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 552..557
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 568..573
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 585..593
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 598..602
FT /evidence="ECO:0007829|PDB:7ODH"
SQ SEQUENCE 618 AA; 68795 MW; 8899BA7486865D3F CRC64;
MSAYATQGFN LDDRGRRIVV DPVTRIEGHM RCEVNVDANN VIRNAVSTGT MWRGLEVILK
GRDPRDAWAF VERICGVCTG CHALASVRAV ENALDIRIPK NAHLIREIMA KTLQVHDHAV
HFYHLHALDW VDVMSALKAD PKRTSELQQL VSPAHPLSSA GYFRDIQNRL KRFVESGQLG
PFMNGYWGSK AYVLPPEANL MAVTHYLEAL DLQKEWVKIH TIFGGKNPHP NYLVGGVPCA
INLDGIGAAS APVNMERLSF VKARIDEIIE FNKNVYVPDV LAIGTLYKQA GWLYGGGLAA
TNVLDYGEYP NVAYNKSTDQ LPGGAILNGN WDEVFPVDPR DSQQVQEFVS HSWYKYADES
VGLHPWDGVT EPNYVLGANT KGTRTRIEQI DESAKYSWIK SPRWRGHAME VGPLSRYILA
YAHARSGNKY AERPKEQLEY SAQMINSAIP KALGLPETQY TLKQLLPSTI GRTLARALES
QYCGEMMHSD WHDLVANIRA GDTATANVDK WDPATWPLQA KGVGTVAAPR GALGHWIRIK
DGRIENYQCV VPTTWNGSPR DYKGQIGAFE ASLMNTPMVN PEQPVEILRT LHSFDPCLAC
STHVMSAEGQ ELTTVKVR
