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Protein

Nitrogenase iron protein 2

Gene

nifH2

Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.

Catalytic activityi

8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate.

Cofactori

[4Fe-4S] clusterNote: Binds 1 [4Fe-4S] cluster per dimer.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi100Iron-sulfur (4Fe-4S); shared with dimeric partnerBy similarity1
Metal bindingi134Iron-sulfur (4Fe-4S); shared with dimeric partnerBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 19ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrogen fixation

Keywords - Ligandi

4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciAVAR240292:G7WH-9715-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogenase iron protein 2 (EC:1.18.6.1)
Alternative name(s):
Nitrogenase Fe protein 2
Nitrogenase component II
Nitrogenase reductase
Gene namesi
Name:nifH2
Ordered Locus Names:Ava_4247
OrganismiAnabaena variabilis (strain ATCC 29413 / PCC 7937)
Taxonomic identifieri240292 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena
Proteomesi
  • UP000002533 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001394841 – 296Nitrogenase iron protein 2Add BLAST296

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei103ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferaseBy similarity1

Post-translational modificationi

The reversible ADP-ribosylation of Arg-103 inactivates the nitrogenase reductase and regulates nitrogenase activity.By similarity

Keywords - PTMi

ADP-ribosylation

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi240292.Ava_4247.

Structurei

3D structure databases

ProteinModelPortaliQ44484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NifH/BchL/ChlL family.Curated

Phylogenomic databases

eggNOGiENOG4105DSM. Bacteria.
COG1348. LUCA.
HOGENOMiHOG000228826.
KOiK02588.
OMAiYQGVKCV.
OrthoDBiPOG091H0230.

Family and domain databases

CDDicd02040. NifH. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00533. NifH. 1 hit.
InterProiIPR030655. NifH/chlL_CS.
IPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR005977. Nitrogenase_Fe_NifH.
IPR027417. P-loop_NTPase.
[Graphical view]
PIRSFiPIRSF000363. Nitrogenase_iron. 1 hit.
PRINTSiPR00091. NITROGNASEII.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01287. nifH. 1 hit.
PROSITEiPS00746. NIFH_FRXC_1. 1 hit.
PS00692. NIFH_FRXC_2. 1 hit.
PS51026. NIFH_FRXC_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q44484-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIDNIRQIAF YGKGGIGKST TSQNTIAGLA EMGERIMIVG CDPKADSTRL
60 70 80 90 100
MLHSKAQTTI LHLAAERGAV EDLELDEVLL TGYQGVKCVE SGGPEPGVGC
110 120 130 140 150
AGRGIITAIN FLEENGAYED LDFVSYDVLG DVVCGGFAMP IREGKAQEIY
160 170 180 190 200
IVCSGEMMAM YAANNIARGI LKYAHSGGVR LGGLICNSRN VDREVELIEA
210 220 230 240 250
LAERLNTQMI HFVPRNNVVQ HAELRRMTVI EYATEHPQAN EYRTLAKKIK
260 270 280 290
ENTKLTIPTP ISMDELEELL VEFGILGGEE EYQKAIAQDA GKAVVV
Length:296
Mass (Da):32,208
Last modified:April 4, 2006 - v2
Checksum:i761CB9AB74697B1F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti171L → W in AAA93020 (PubMed:7568132).Curated1
Sequence conflicti202A → V in AAA93020 (PubMed:7568132).Curated1
Sequence conflicti283Q → P in AAA93020 (PubMed:7568132).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49859 Genomic DNA. Translation: AAA93020.1.
U25160 Genomic DNA. Translation: AAC43540.1.
CP000117 Genomic DNA. Translation: ABA23846.1.
PIRiS70251.

Genome annotation databases

EnsemblBacteriaiABA23846; ABA23846; Ava_4247.
KEGGiava:Ava_4247.
PATRICi35429857. VBIAnaVar43351_5457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49859 Genomic DNA. Translation: AAA93020.1.
U25160 Genomic DNA. Translation: AAC43540.1.
CP000117 Genomic DNA. Translation: ABA23846.1.
PIRiS70251.

3D structure databases

ProteinModelPortaliQ44484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi240292.Ava_4247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA23846; ABA23846; Ava_4247.
KEGGiava:Ava_4247.
PATRICi35429857. VBIAnaVar43351_5457.

Phylogenomic databases

eggNOGiENOG4105DSM. Bacteria.
COG1348. LUCA.
HOGENOMiHOG000228826.
KOiK02588.
OMAiYQGVKCV.
OrthoDBiPOG091H0230.

Enzyme and pathway databases

BioCyciAVAR240292:G7WH-9715-MONOMER.

Family and domain databases

CDDicd02040. NifH. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00533. NifH. 1 hit.
InterProiIPR030655. NifH/chlL_CS.
IPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR005977. Nitrogenase_Fe_NifH.
IPR027417. P-loop_NTPase.
[Graphical view]
PIRSFiPIRSF000363. Nitrogenase_iron. 1 hit.
PRINTSiPR00091. NITROGNASEII.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01287. nifH. 1 hit.
PROSITEiPS00746. NIFH_FRXC_1. 1 hit.
PS00692. NIFH_FRXC_2. 1 hit.
PS51026. NIFH_FRXC_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNIFH2_ANAVT
AccessioniPrimary (citable) accession number: Q44484
Secondary accession number(s): Q3M590, Q44469
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: April 4, 2006
Last modified: November 2, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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.