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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)DescriptionActionsGraphical viewLength
Metal bindingi98Iron-sulfur (2Fe-2S)By similarity1
Metal bindingi103Iron-sulfur (2Fe-2S)By similarity1
Metal bindingi139Iron-sulfur (2Fe-2S)By similarity1
Metal bindingi143Iron-sulfur (2Fe-2S)By similarity1

GO - Molecular functioni

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

Keywordsi

Molecular functionOxidoreductase
Ligand2Fe-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)DescriptionActionsGraphical viewLength
ChainiPRO_00004187161 – 171NADP-reducing hydrogenase subunit HndAAdd BLAST171

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

Structurei

Secondary structure

1171
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi101 – 104Combined sources4
Turni105 – 107Combined sources3
Helixi108 – 119Combined sources12
Beta strandi122 – 129Combined sources8
Beta strandi135 – 142Combined sources8
Helixi152 – 154Combined sources3
Beta strandi159 – 162Combined sources4
Helixi163 – 170Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AUVNMR-A87-171[»]
ProteinModelPortaliQ46505.
SMRiQ46505.
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.
KOiK18330.

Family and domain databases

CDDicd03064. TRX_Fd_NuoE. 1 hit.
InterProiView protein in InterPro
IPR028431. NADP_DH_HndA.
IPR002023. NuoE-like.
IPR036249. Thioredoxin-like_sf.
PANTHERiPTHR43342:SF2. PTHR43342:SF2. 1 hit.
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.

Genome annotation databases

KEGGiag:AAA87054.

Similar proteinsi

Entry informationi

Entry nameiHNDA_DESFR
AccessioniPrimary (citable) accession number: Q46505
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: November 1, 1996
Last modified: October 25, 2017
This is version 84 of the entry and version 1 of the sequence. See 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