ID   HNDC_SOLFR              Reviewed;         490 AA.
AC   Q46507;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=NADP-reducing hydrogenase subunit HndC;
DE            EC=1.12.1.3 {ECO:0000269|PubMed:9703971};
DE   AltName: Full=Hydrogen dehydrogenase (NADP(+));
GN   Name=hndC;
OS   Solidesulfovibrio fructosivorans (Desulfovibrio fructosivorans).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Solidesulfovibrio.
OX   NCBI_TaxID=878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A NADP-REDUCING HYDROGENASE,
RP   AND DISRUPTION PHENOTYPE.
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       HndC is probably the reducing subunit. {ECO:0000269|PubMed:9703971}.
CC   -!- DISRUPTION PHENOTYPE: Disruption completely abolishes the NADP
CC       reductase activity. {ECO:0000269|PubMed:7751270}.
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; U07229; AAA87056.1; -; Genomic_DNA.
DR   PIR; C57150; C57150.
DR   AlphaFoldDB; Q46507; -.
DR   SMR; Q46507; -.
DR   PRIDE; Q46507; -.
DR   KEGG; ag:AAA87056; -.
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:0050583; F:hydrogen dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   Gene3D; 1.20.1440.230; -; 1.
DR   Gene3D; 3.40.50.11540; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR   InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF00037; Fer4; 2.
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   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Repeat.
FT   CHAIN           1..490
FT                   /note="NADP-reducing hydrogenase subunit HndC"
FT                   /id="PRO_0000418717"
FT   DOMAIN          433..462
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          463..490
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ   SEQUENCE   490 AA;  52586 MW;  60DFF36F0FA220A6 CRC64;
     MAATTTEKKQ LRIATRNCGF IDPESIDDYI ALRGYEGLAK VLTMTPAEVV DLVKRSGLRG
     RGGAGFPTGI KWGIALGNKA DQKYMVCNAD EGDPEFMDRA VLEGDPHSVV EAMAIGGYAI
     GATRGTVYIR AEYPLAIKRL KKAIDDAREY GLLGENIFGS GFDFDIELKY GAGAFVCGEE
     TALIRSMEGK RGEPVTKPPF PAQSGYWEKP TIVNNVETFA NIPAIIINGA DWFSGIGTAT
     SKGTKVFALA GKIQNVGLIE VPMGISLREV IFDIGGGCPD GKAFKAVQTG GPSGGALANK
     DLDVAIDYES LAACKSIMGS GGMVVMDEDD CMVSVAKFFL DFTMDETCGK CTPCRIGSKR
     LYEILDRITK GKGTRADLDR LKSLSEIIKD TALCGLGQTM PNPILSTMDT FANEYEAHVD
     DKKCPAHVCT ALLTYTIDPA KCTGCGLCTR VCPVECISGT KKQPHTIDTT RCIKCGACYD
     KCKFDSIIKQ