HOXH_CUPNH
ID HOXH_CUPNH Reviewed; 488 AA.
AC P22320; Q7WXN0;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=NAD-reducing hydrogenase HoxS subunit beta;
DE EC=1.12.1.2;
GN Name=hoxH; OrderedLocusNames=PHG091;
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=2188945; DOI=10.1128/jb.172.6.2920-2929.1990;
RA Tran-Betcke A., Warnecke U., Boecker C., Zaborosch C., Friedrich B.;
RT "Cloning and nucleotide sequences of the genes for the subunits of NAD-
RT reducing hydrogenase of Alcaligenes eutrophus H16.";
RL J. Bacteriol. 172:2920-2929(1990).
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 2-39.
RX PubMed=2496982; DOI=10.1111/j.1432-1033.1989.tb14708.x;
RA Zaborosch C., Schneider K., Schlegel H.G., Kratzin H.;
RT "Comparison of the NH2-terminal amino acid sequences of the four non-
RT identical subunits of the NAD-linked hydrogenases from Nocardia opaca 1b
RT and Alcaligenes eutrophus H16.";
RL Eur. J. Biochem. 181:175-180(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2 + NAD(+) = H(+) + NADH; Xref=Rhea:RHEA:24636,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.12.1.2;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC -!- SUBUNIT: Tetramer of an alpha and a gamma subunits (flavin-containing
CC dimer), and a delta and a nickel-containing beta subunits (hydrogenase
CC dimer).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000305}.
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DR EMBL; M55230; AAC06143.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP85844.1; -; Genomic_DNA.
DR PIR; D35385; D35385.
DR RefSeq; WP_011154013.1; NZ_CP039289.1.
DR AlphaFoldDB; P22320; -.
DR SMR; P22320; -.
DR IntAct; P22320; 1.
DR STRING; 381666.PHG091; -.
DR EnsemblBacteria; AAP85844; AAP85844; PHG091.
DR GeneID; 39976751; -.
DR KEGG; reh:PHG091; -.
DR PATRIC; fig|381666.6.peg.68; -.
DR eggNOG; COG3259; Bacteria.
DR HOGENOM; CLU_044556_0_0_4; -.
DR OMA; QNNLAMN; -.
DR OrthoDB; 1967820at2; -.
DR BioCyc; MetaCyc:HOXHALCA-MON; -.
DR BRENDA; 1.12.1.2; 231.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0047985; F:hydrogen dehydrogenase 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; 2.
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 Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Nickel;
KW Oxidoreductase; Plasmid; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2496982"
FT CHAIN 2..488
FT /note="NAD-reducing hydrogenase HoxS subunit beta"
FT /id="PRO_0000199719"
FT BINDING 62
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 65
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 458
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 461
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT CONFLICT 30
FT /note="V -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="A -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="V -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="N -> H (in Ref. 1; AAC06143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 54863 MW; 751C509483818E6A CRC64;
MSRKLVIDPV TRIEGHGKVV VHLDDDNKVV DAKLHVVEFR GFEKFVQGHP FWEAPMFLQR
ICGICFVSHH LCGAKALDDM VGVGLKSGIH VTPTAEKMRR LGHYAQMLQS HTTAYFYLIV
PEMLFGMDAP PAQRNVLGLI EANPDLVKRV VMLRKWGQEV IKAVFGKKMH GINSVPGGVN
NNLSIAERDR FLNGEEGLLS VDQVIDYAQD GLRLFYDFHQ KHRAQVDSFA DVPALSMCLV
GDDDNVDYYH GRLRIIDDDK HIVREFDYHD YLDHFSEAVE EWSYMKFPYL KELGREQGSV
RVGPLGRMNV TKSLPTPLAQ EALERFHAYT KGRTNNMTLH TNWARAIEIL HAAEVVKELL
HDPDLQKDQL VLTPPPNAWT GEGVGVVEAP RGTLLHHYRA DERGNITFAN LVVATTQNNQ
VMNRTVRSVA EDYLGGHGEI TEGMMNAIEV GIRAYDPCLS CATHALGQMP LVVSVFDAAG
RLIDERAR
