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Protein

NADP-reducing hydrogenase subunit HndA

Gene

hndA

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.

Cofactori

[2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster.By similarity

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi98 – 981Iron-sulfur (2Fe-2S)By similarity
Metal bindingi103 – 1031Iron-sulfur (2Fe-2S)By similarity
Metal bindingi139 – 1391Iron-sulfur (2Fe-2S)By similarity
Metal bindingi143 – 1431Iron-sulfur (2Fe-2S)By similarity

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB
  • hydrogen dehydrogenase (NADP+) activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding, NADP

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 171171NADP-reducing hydrogenase subunit HndAPRO_0000418716Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of HndA, HndB, HndC and HndD subunits. HndA and HndB could form a heterodimeric intermediate in the electron transfer between the active site of hydrogenase subunit HndD and the NADP reduction site of the reducing subunit HndC.2 Publications

Protein-protein interaction databases

STRINGi596151.DesfrDRAFT_0398.

Structurei

Secondary structure

1
171
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi101 – 1044Combined sources
Turni105 – 1073Combined sources
Helixi108 – 11912Combined sources
Beta strandi122 – 1298Combined sources
Beta strandi135 – 1428Combined sources
Helixi152 – 1543Combined sources
Beta strandi159 – 1624Combined sources
Helixi163 – 1708Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AUVNMR-A87-171[»]
ProteinModelPortaliQ46505.
SMRiQ46505. Positions 87-171.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ46505.

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I 24 kDa subunit family.Curated

Phylogenomic databases

eggNOGiENOG410902H. Bacteria.
COG1905. LUCA.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002023. NuoE-like.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PIRSFiPIRSF000216. NADH_DH_24kDa. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.

Sequencei

Sequence statusi: Complete.

Q46505-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNSTCQAVG ECRVPEHAVL PQPLYREVVQ FIESLPQKEG HLVTVLHKAQ
60 70 80 90 100
SVFGYLPIEV QQFVADHMEV PLAQVYGVVS FYTFFTMVPK GKYPISVCMG
110 120 130 140 150
TACFVKGADK VVHAFKEQLK IDIGDVTPDG RFSIDTLRCV GGCALAPIVM
160 170
VGEKVYGNVT PGQVKKILAE Y
Length:171
Mass (Da):18,807
Last modified:November 1, 1996 - v1
Checksum:i96D11A2A82AAB0C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07229 Genomic DNA. Translation: AAA87054.1.
PIRiA57150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07229 Genomic DNA. Translation: AAA87054.1.
PIRiA57150.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AUVNMR-A87-171[»]
ProteinModelPortaliQ46505.
SMRiQ46505. Positions 87-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi596151.DesfrDRAFT_0398.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410902H. Bacteria.
COG1905. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ46505.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002023. NuoE-like.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PIRSFiPIRSF000216. NADH_DH_24kDa. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHNDA_DESFR
AccessioniPrimary (citable) accession number: Q46505
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.