HOXU_CUPNH
ID HOXU_CUPNH Reviewed; 234 AA.
AC P22318;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=NAD-reducing hydrogenase HoxS subunit gamma;
DE EC=1.12.1.2;
GN Name=hoxU; OrderedLocusNames=PHG089;
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 2-26.
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00465};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000305};
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 complex I 75 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; M55230; AAC06141.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP85842.1; -; Genomic_DNA.
DR PIR; B35385; B35385.
DR RefSeq; WP_011154011.1; NZ_CP039289.1.
DR AlphaFoldDB; P22318; -.
DR SMR; P22318; -.
DR STRING; 381666.PHG089; -.
DR EnsemblBacteria; AAP85842; AAP85842; PHG089.
DR GeneID; 39976413; -.
DR KEGG; reh:PHG089; -.
DR PATRIC; fig|381666.6.peg.66; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_11_3_4; -.
DR OMA; NHVCAVC; -.
DR OrthoDB; 323168at2; -.
DR BioCyc; MetaCyc:HOXUALCA-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:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051537; F:2 iron, 2 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 GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR016214; NAD-red_Hydgase_HoxS_gsu.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF000309; NAD_red_hyd_HoxU; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Cytoplasm; Direct protein sequencing; Flavoprotein; FMN;
KW Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2496982"
FT CHAIN 2..234
FT /note="NAD-reducing hydrogenase HoxS subunit gamma"
FT /id="PRO_0000118538"
FT DOMAIN 2..77
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 77..116
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 35
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 61
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 97
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 234 AA; 26173 MW; 38E59021F7B82A2E CRC64;
MSIQITIDGK TLTTEEGRTL VDVAAENGVY IPTLCYLKDK PCLGTCRVCS VKVNGNVAAA
CTVRVSKGLN VEVNDPELVD MRKALVEFLF AEGNHNCPSC EKSGRCQLQA VGYEVDMMVS
RFPYRFPVRV VDHASEKIWL ERDRCIFCQR CVEFIRDKAS GRKIFSISHR GPESRIEIDA
ELANAMPPEQ VKEAVAICPV GTILEKRVGY DDPIGRRKYE IQSVRARALE GEDK
