ID   HOXY_CUPNH              Reviewed;         209 AA.
AC   P22319;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=NAD-reducing hydrogenase HoxS subunit delta;
DE            EC=1.12.1.2;
GN   Name=hoxY; OrderedLocusNames=PHG090;
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 1-20.
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 2 [4Fe-4S] clusters.;
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC       Note=Binds 1 [3Fe-4S] cluster.;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC       Note=Binds 1 [2Fe-2S] cluster.;
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.
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DR   EMBL; M55230; AAC06142.1; -; Genomic_DNA.
DR   EMBL; AY305378; AAP85843.1; -; Genomic_DNA.
DR   PIR; C35385; C35385.
DR   AlphaFoldDB; P22319; -.
DR   SMR; P22319; -.
DR   STRING; 381666.PHG090; -.
DR   EnsemblBacteria; AAP85843; AAP85843; PHG090.
DR   KEGG; reh:PHG090; -.
DR   eggNOG; COG1941; Bacteria.
DR   HOGENOM; CLU_093095_0_0_4; -.
DR   OMA; CNAENVH; -.
DR   BioCyc; MetaCyc:HOXYALCA-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:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0047985; F:hydrogen dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.700; -; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR037024; NiFe_Hase_small_N_sf.
DR   Pfam; PF01058; Oxidored_q6; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3Fe-4S; 4Fe-4S; Cytoplasm; Direct protein sequencing; Iron;
KW   Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..209
FT                   /note="NAD-reducing hydrogenase HoxS subunit delta"
FT                   /id="PRO_0000199734"
SQ   SEQUENCE   209 AA;  22881 MW;  247505ED38604686 CRC64;
     MRAPHKDEIA SHELPATPMD PALAANREGK IKVATIGLCG CWGCTLSFLD MDERLLPLLE
     KVTLLRSSLT DIKRIPERCA IGFVEGGVSS EENIETLEHF RENCDILISV GACAVWGGVP
     AMRNVFELKD CLAEAYVNSA TAVPGAKAVV PFHPDIPRIT TKVYPCHEVV KMDYFIPGCP
     PDGDAIFKVL DDLVNGRPFD LPSSINRYD