HNDA_SOLFR
ID HNDA_SOLFR Reviewed; 171 AA.
AC Q46505;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=NADP-reducing hydrogenase subunit HndA;
DE EC=1.12.1.3 {ECO:0000269|PubMed:9703971};
DE AltName: Full=Hydrogen dehydrogenase (NADP(+));
GN Name=hndA;
OS Solidesulfovibrio fructosivorans (Desulfovibrio fructosivorans).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Solidesulfovibrio.
OX NCBI_TaxID=878;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7751270; DOI=10.1128/jb.177.10.2628-2636.1995;
RA Malki S., Saimmaime I., De Luca G., Rousset M., Dermoun Z., Belaich J.P.;
RT "Characterization of an operon encoding an NADP-reducing hydrogenase in
RT Desulfovibrio fructosovorans.";
RL J. Bacteriol. 177:2628-2636(1995).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=9703971; DOI=10.1006/bbrc.1998.9022;
RA de Luca G., de Philip P., Rousset M., Belaich J.P., Dermoun Z.;
RT "The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: evidence
RT for a native complex with hydrogen-dependent methyl-viologen-reducing
RT activity.";
RL Biochem. Biophys. Res. Commun. 248:591-596(1998).
RN [3]
RP STRUCTURE BY NMR OF 87-171 IN COMPLEX WITH IRON-SULFUR (2FE-2S), AND
RP SUBUNIT.
RX PubMed=16731971; DOI=10.1110/ps.051916606;
RA Nouailler M., Morelli X., Bornet O., Chetrit B., Dermoun Z.,
RA Guerlesquin F.;
RT "Solution structure of HndAc: a thioredoxin-like domain involved in the
RT NADP-reducing hydrogenase complex.";
RL Protein Sci. 15:1369-1378(2006).
CC -!- FUNCTION: Catalyzes the reduction of NADP in the presence of molecular
CC H(2) to yield NADPH. {ECO:0000269|PubMed:7751270,
CC ECO:0000269|PubMed:9703971}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2 + NADP(+) = H(+) + NADPH; Xref=Rhea:RHEA:18637,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.12.1.3;
CC Evidence={ECO:0000269|PubMed:9703971};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by oxygen. {ECO:0000269|PubMed:9703971}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for NADP (at 30 degrees Celsius and at pH 8)
CC {ECO:0000269|PubMed:9703971};
CC Vmax=0.013 umol/min/mg enzyme (at 30 degrees Celsius and at pH 8)
CC {ECO:0000269|PubMed:9703971};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:9703971};
CC -!- SUBUNIT: Heterotetramer composed of HndA, HndB, HndC and HndD subunits.
CC HndA and HndB could form a heterodimeric intermediate in the electron
CC transfer between the active site of hydrogenase subunit HndD and the
CC NADP reduction site of the reducing subunit HndC.
CC {ECO:0000269|PubMed:16731971, ECO:0000269|PubMed:9703971}.
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; U07229; AAA87054.1; -; Genomic_DNA.
DR PIR; A57150; A57150.
DR PDB; 2AUV; NMR; -; A=87-171.
DR PDBsum; 2AUV; -.
DR AlphaFoldDB; Q46505; -.
DR SMR; Q46505; -.
DR KEGG; ag:AAA87054; -.
DR EvolutionaryTrace; Q46505; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0050583; F:hydrogen dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.10.10.1590; -; 1.
DR InterPro; IPR028431; NADP_DH_HndA.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43342:SF2; PTHR43342:SF2; 1.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Iron; Iron-sulfur; Metal-binding; NADP;
KW Oxidoreductase.
FT CHAIN 1..171
FT /note="NADP-reducing hydrogenase subunit HndA"
FT /id="PRO_0000418716"
FT BINDING 98
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:2AUV"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2AUV"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:2AUV"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:2AUV"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:2AUV"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:2AUV"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2AUV"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:2AUV"
SQ SEQUENCE 171 AA; 18807 MW; 96D11A2A82AAB0C4 CRC64;
MQNSTCQAVG ECRVPEHAVL PQPLYREVVQ FIESLPQKEG HLVTVLHKAQ SVFGYLPIEV
QQFVADHMEV PLAQVYGVVS FYTFFTMVPK GKYPISVCMG TACFVKGADK VVHAFKEQLK
IDIGDVTPDG RFSIDTLRCV GGCALAPIVM VGEKVYGNVT PGQVKKILAE Y
