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Protein

NADP-reducing hydrogenase subunit HndC

Gene

hndC

Organism
Desulfovibrio fructosivorans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of NADP in the presence of molecular H2 to yield NADPH.2 Publications

Catalytic activityi

H2 + NADP+ = H+ + NADPH.

Enzyme regulationi

Inhibited by oxygen.1 Publication

Kineticsi

  1. KM=0.09 mM for NADP (at 30 degrees Celsius and at pH 8)1 Publication
  1. Vmax=0.013 µmol/min/mg enzyme (at 30 degrees Celsius and at pH 8)1 Publication

pH dependencei

Optimum pH is 8.1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-reducing hydrogenase subunit HndC (EC:1.12.1.3)
Alternative name(s):
Hydrogen dehydrogenase (NADP(+))
Gene namesi
Name:hndC
OrganismiDesulfovibrio fructosivorans
Taxonomic identifieri878 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Pathology & Biotechi

Disruption phenotypei

Disruption completely abolishes the NADP reductase activity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490NADP-reducing hydrogenase subunit HndCPRO_0000418717Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of HndA, HndB, HndC and HndD subunits. HndC is probably the reducing subunit.1 Publication

Protein-protein interaction databases

STRINGi596151.DesfrDRAFT_0400.

Structurei

3D structure databases

ProteinModelPortaliQ46507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini433 – 462304Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini463 – 490284Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the complex I 51 kDa subunit family.Curated
Contains 2 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4107QIZ. Bacteria.
COG1145. LUCA.
COG1894. LUCA.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR001949. NADH-UbQ_OxRdtase_51kDa_CS.
IPR011538. Nuo51_FMN-bd.
IPR019575. Nuop51_4Fe4S-bd.
[Graphical view]
PfamiPF01512. Complex1_51K. 1 hit.
PF00037. Fer4. 2 hits.
PF10589. NADH_4Fe-4S. 1 hit.
[Graphical view]
SMARTiSM00928. NADH_4Fe-4S. 1 hit.
[Graphical view]
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
PS00645. COMPLEX1_51K_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q46507-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATTTEKKQ LRIATRNCGF IDPESIDDYI ALRGYEGLAK VLTMTPAEVV
60 70 80 90 100
DLVKRSGLRG RGGAGFPTGI KWGIALGNKA DQKYMVCNAD EGDPEFMDRA
110 120 130 140 150
VLEGDPHSVV EAMAIGGYAI GATRGTVYIR AEYPLAIKRL KKAIDDAREY
160 170 180 190 200
GLLGENIFGS GFDFDIELKY GAGAFVCGEE TALIRSMEGK RGEPVTKPPF
210 220 230 240 250
PAQSGYWEKP TIVNNVETFA NIPAIIINGA DWFSGIGTAT SKGTKVFALA
260 270 280 290 300
GKIQNVGLIE VPMGISLREV IFDIGGGCPD GKAFKAVQTG GPSGGALANK
310 320 330 340 350
DLDVAIDYES LAACKSIMGS GGMVVMDEDD CMVSVAKFFL DFTMDETCGK
360 370 380 390 400
CTPCRIGSKR LYEILDRITK GKGTRADLDR LKSLSEIIKD TALCGLGQTM
410 420 430 440 450
PNPILSTMDT FANEYEAHVD DKKCPAHVCT ALLTYTIDPA KCTGCGLCTR
460 470 480 490
VCPVECISGT KKQPHTIDTT RCIKCGACYD KCKFDSIIKQ
Length:490
Mass (Da):52,586
Last modified:November 1, 1996 - v1
Checksum:i60DFF36F0FA220A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07229 Genomic DNA. Translation: AAA87056.1.
PIRiC57150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07229 Genomic DNA. Translation: AAA87056.1.
PIRiC57150.

3D structure databases

ProteinModelPortaliQ46507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi596151.DesfrDRAFT_0400.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QIZ. Bacteria.
COG1145. LUCA.
COG1894. LUCA.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR001949. NADH-UbQ_OxRdtase_51kDa_CS.
IPR011538. Nuo51_FMN-bd.
IPR019575. Nuop51_4Fe4S-bd.
[Graphical view]
PfamiPF01512. Complex1_51K. 1 hit.
PF00037. Fer4. 2 hits.
PF10589. NADH_4Fe-4S. 1 hit.
[Graphical view]
SMARTiSM00928. NADH_4Fe-4S. 1 hit.
[Graphical view]
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
PS00645. COMPLEX1_51K_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans."
    Malki S., Saimmaime I., De Luca G., Rousset M., Dermoun Z., Belaich J.P.
    J. Bacteriol. 177:2628-2636(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A NADP-REDUCING HYDROGENASE, DISRUPTION PHENOTYPE.
  2. "The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity."
    de Luca G., de Philip P., Rousset M., Belaich J.P., Dermoun Z.
    Biochem. Biophys. Res. Commun. 248:591-596(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A NADP-REDUCING HYDROGENASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.

Entry informationi

Entry nameiHNDC_DESFR
AccessioniPrimary (citable) accession number: Q46507
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.