ID   HNDB_SOLFR              Reviewed;         126 AA.
AC   Q46506;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=NADP-reducing hydrogenase subunit HndB;
DE            EC=1.12.1.3 {ECO:0000269|PubMed:9703971};
DE   AltName: Full=Hydrogen dehydrogenase (NADP(+));
GN   Name=hndB;
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 AS A NADP-REDUCING
RP   HYDROGENASE.
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 AS A NADP-REDUCING HYDROGENASE, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY 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).
CC   -!- FUNCTION: Catalyzes the reduction of NADP in the presence of molecular
CC       H2 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   -!- 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:9703971}.
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DR   EMBL; U07229; AAA87055.1; -; Genomic_DNA.
DR   PIR; B57150; B57150.
DR   AlphaFoldDB; Q46506; -.
DR   SMR; Q46506; -.
DR   KEGG; ag:AAA87055; -.
DR   GO; GO:0050583; F:hydrogen dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..126
FT                   /note="NADP-reducing hydrogenase subunit HndB"
FT                   /id="PRO_0000418719"
SQ   SEQUENCE   126 AA;  13791 MW;  B05A33FEE66012CC CRC64;
     MSTIRSFEDL KAKRQEILDR KAARNGKTII NVSLATCSIA AGGKVAMEAM QDEVAKNGLT
     GVEFMQSSCM TYCYAEPTVE ITLPGKDPVV FGGVDENRAR ELVTEYVMKG EPVEGIIPVN
     YERVVL