HOXF_CUPNH
ID HOXF_CUPNH Reviewed; 602 AA.
AC P22317;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=NAD-reducing hydrogenase HoxS subunit alpha;
DE EC=1.12.1.2;
GN Name=hoxF; OrderedLocusNames=PHG088;
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 1-27.
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 -!- FUNCTION: Subunits alpha and gamma of HoxS constitute an NADH--
CC oxidoreductase.
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; Evidence={ECO:0000305};
CC Note=Binds 1 FMN. {ECO:0000305};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Tetramer of an alpha and a gamma subunits (flavin-containing
CC dimer), and a delta and a nickel-containing beta subunit (hydrogenase
CC dimer).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; M55230; AAC06140.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP85841.1; -; Genomic_DNA.
DR PIR; A35385; A35385.
DR RefSeq; WP_011154010.1; NZ_CP039289.1.
DR AlphaFoldDB; P22317; -.
DR SMR; P22317; -.
DR STRING; 381666.PHG088; -.
DR PRIDE; P22317; -.
DR EnsemblBacteria; AAP85841; AAP85841; PHG088.
DR GeneID; 39976412; -.
DR KEGG; reh:PHG088; -.
DR PATRIC; fig|381666.6.peg.65; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_2_4; -.
DR OMA; CDQGPAL; -.
DR OrthoDB; 688908at2; -.
DR BioCyc; MetaCyc:HOXFALCA-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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0047985; F:hydrogen dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR Gene3D; 1.10.10.1590; -; 1.
DR Gene3D; 1.20.1440.230; -; 1.
DR Gene3D; 3.40.50.11540; -; 1.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF140490; SSF140490; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Direct protein sequencing; Flavoprotein; FMN; Iron;
KW Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid;
KW Reference proteome.
FT CHAIN 1..602
FT /note="NAD-reducing hydrogenase HoxS subunit alpha"
FT /id="PRO_0000118564"
FT BINDING 219..228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 332..379
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 502
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 505
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 545
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT CONFLICT 24
FT /note="W -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 66784 MW; B7D9BBB11AB53F6C CRC64;
MDSRITTILE RYRSDRTRLI DILWDVQHEY GHIPDAVLPQ LGAGLKLSPL DIRETASFYH
FFLDKPSGKY RIYLCNSVIA KINGYQAVRE ALERETGIRF GETDPNGMFG LFDTPCIGLS
DQEPAMLIDK VVFTRLRPGK ITDIIAQLKQ GRSPAEIANP AGLPSQDIAY VDAMVESNVR
TKGPVFFRGR TDLRSLLDQC LLLKPEQVIE TIVDSRLRGR GGAGFSTGLK WRLCRDAESE
QKYVICNADE GEPGTFKDRV LLTRAPKKVF VGMVIAAYAI GCRKGIVYLR GEYFYLKDYL
ERQLQELRED GLLGRAIGGR AGFDFDIRIQ MGAGAYICGD ESALIESCEG KRGTPRVKPP
FPVQQGYLGK PTSVNNVETF AAVSRIMEEG ADWFRAMGTP DSAGTRLLSV AGDCSKPGIY
EVEWGVTLNE VLAMVGARDA RAVQISGPSG ECVSVAKDGE RKLAYEDLSC NGAFTIFNCK
RDLLEIVRDH MQFFVEESCG ICVPCRAGNV DLHRKVEWVI AGKACQKDLD DMVSWGALVR
RTSRCGLGAT SPKPILTTLE KFPEIYQNKL VRHEGPLLPS FDLDTALGGY EKALKDLEEV
TR
