HNDD_SOLFR
ID HNDD_SOLFR Reviewed; 585 AA.
AC Q46508;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=NADP-reducing hydrogenase subunit HndD;
DE EC=1.12.1.3 {ECO:0000269|PubMed:9703971};
DE AltName: Full=Hydrogen dehydrogenase (NADP(+));
GN Name=hndD;
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 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01184};
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 HndD is probably the hydrogenase subunit. {ECO:0000269|PubMed:9703971}.
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DR EMBL; U07229; AAA87057.1; -; Genomic_DNA.
DR PIR; D57150; D57150.
DR AlphaFoldDB; Q46508; -.
DR SMR; Q46508; -.
DR KEGG; ag:AAA87057; -.
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:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0050583; F:hydrogen dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 4.10.260.20; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR InterPro; IPR003149; Fe_hydrogenase_ssu.
DR InterPro; IPR036991; Fe_hydrogenase_ssu_sf.
DR InterPro; IPR013352; Fe_hydrogenase_subset.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF02256; Fe_hyd_SSU; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00902; Fe_hyd_SSU; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF53920; SSF53920; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR02512; FeFe_hydrog_A; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase;
KW Repeat.
FT CHAIN 1..585
FT /note="NADP-reducing hydrogenase subunit HndD"
FT /id="PRO_0000418718"
FT DOMAIN 2..85
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 85..124
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 144..174
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 185..216
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 36
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 55
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
SQ SEQUENCE 585 AA; 63429 MW; C14D0EF6AA3E2A72 CRC64;
MSMLTITIDG KTTSVPEGST ILDAAKTLDI DIPTLCYLNL EALSINNKAA SCRVCVVEVE
GRRNLAPSCA TPVTDNMVVK TNSLRVLNAR RTVLELLLSD HPKDCLVCAK SGECELQTLA
ERFGIRESPY DGGEMSHYRK DISASIIRDM DKCIMCRRCE TMCNTVQTCG VLSGVNRGFT
AVVAPAFEMN LADTVCTNCG QCVAVCPTGA LVEHEYIWEV VEALANPDKV VIVQTAPAVR
AALGEDLGVA PGTSVTGKMA AALRRLGFDH VFDTDFAADL TIMEEGSEFL DRLGKHLAGD
TNVKLPILTS CCPGWVKFFE HQFPDMLDVP STAKSPQQMF GAIAKTYYAD LLGIPREKLV
VVSVMPCLAK KYECARPEFS VNGNPDVDIV ITTRELAKLV KRMNIDFAGL PDEDFDAPLG
ASTGAAPIFG VTGGVIEAAL RTAYELATGE TLKKVDFEDV RGMDGVKKAK VKVGDNELVI
GVAHGLGNAR ELLKPCGAGE TFHAIEVMAC PGGCIGGGGQ PYHHGDVELL KKRTQVLYAE
DAGKPLRKSH ENPYIIELYE KFLGKPLSER SHQLLHTHYF KRQRL
