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Protein

Nitrogenase iron protein 1

Gene

nifH1

Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-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.

Enzyme regulationi

Nitrogenase holoenzyme is subject to 'conformational protection' by FeSII; under oxidizing conditions FeSII binds to the holoenzyme and reversibly protects it from oxidation (PubMed:7830548).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi98Iron-sulfur (4Fe-4S); shared with dimeric partner1
Metal bindingi133Iron-sulfur (4Fe-4S); shared with dimeric partner1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 17ATP8

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • ATP binding Source: UniProtKB-HAMAP
  • carbonyl sulfide nitrogenase activity Source: UniProtKB-EC
  • metal ion binding Source: UniProtKB-KW
  • nitrogenase activity Source: CACAO

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

BioCyciMetaCyc:MONOMER-19495.
BRENDAi1.18.6.1. 49.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogenase iron protein 1 (EC:1.18.6.1)
Alternative name(s):
Nitrogenase Fe protein 1
Nitrogenase component II
Nitrogenase reductase
Gene namesi
Name:nifH1
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16K → Q or P: Loss of nitrogen fixation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001394902 – 290Nitrogenase iron protein 1Add BLAST289

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei101ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferaseBy similarity1

Post-translational modificationi

The reversible ADP-ribosylation of Arg-101 inactivates the nitrogenase reductase and regulates nitrogenase activity.By similarity

Keywords - PTMi

ADP-ribosylation

Expressioni

Inductioni

Constitutively expressed during log and stationary phase in sucrose-limited cultures, its levels decrease during stationary phase (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi322710.Avin_01380.

Structurei

Secondary structure

1290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi12 – 14Combined sources3
Helixi16 – 29Combined sources14
Beta strandi34 – 39Combined sources6
Beta strandi41 – 43Combined sources3
Turni44 – 46Combined sources3
Helixi47 – 50Combined sources4
Beta strandi51 – 53Combined sources3
Helixi58 – 65Combined sources8
Helixi68 – 70Combined sources3
Helixi73 – 75Combined sources3
Beta strandi77 – 80Combined sources4
Helixi81 – 83Combined sources3
Beta strandi85 – 88Combined sources4
Beta strandi96 – 98Combined sources3
Helixi99 – 112Combined sources14
Helixi115 – 117Combined sources3
Beta strandi121 – 127Combined sources7
Helixi129 – 131Combined sources3
Helixi134 – 140Combined sources7
Beta strandi141 – 144Combined sources4
Beta strandi146 – 152Combined sources7
Helixi156 – 175Combined sources20
Beta strandi179 – 186Combined sources8
Beta strandi188 – 190Combined sources3
Helixi193 – 204Combined sources12
Beta strandi208 – 212Combined sources5
Helixi217 – 223Combined sources7
Helixi228 – 231Combined sources4
Beta strandi233 – 235Combined sources3
Helixi236 – 250Combined sources15
Helixi262 – 271Combined sources10
Turni272 – 275Combined sources4
Helixi280 – 282Combined sources3
Turni287 – 289Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DE0X-ray2.40A/B2-290[»]
1FP6X-ray2.15A/B/C/D2-290[»]
1G1MX-ray2.25A/B2-290[»]
1G20X-ray2.20E/F/G/H1-290[»]
1G21X-ray3.00E/F/G/H1-290[»]
1G5PX-ray2.20A/B2-290[»]
1M1YX-ray3.20E/F/G/H/M/N/O/P2-290[»]
1M34X-ray2.30E/F/G/H/M/N/O/P2-290[»]
1N2CX-ray3.00E/F/G/H2-290[»]
1NIPX-ray2.90A/B2-290[»]
1RW4X-ray2.50A2-273[»]
1XCPX-ray3.20A/B/C/D2-290[»]
1XD8X-ray2.70A/B2-290[»]
1XD9X-ray2.80A/B2-290[»]
1XDBX-ray2.80A/B2-290[»]
2AFHX-ray2.10E/F2-290[»]
2AFIX-ray3.10E/F/G/H/M/N/O/P2-290[»]
2C8VX-ray2.50A2-290[»]
2NIPX-ray2.20A/B2-290[»]
4WZAX-ray1.90E/F/G/H2-277[»]
4WZBX-ray2.30E/F/G/H2-273[»]
ProteinModelPortaliP00459.
SMRiP00459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00459.

Family & Domainsi

Sequence similaritiesi

Belongs to the NifH/BchL/ChlL family.Curated

Phylogenomic databases

eggNOGiENOG4105DSM. Bacteria.
COG1348. LUCA.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMRQCAIYG KGGIGKSTTT QNLVAALAEM GKKVMIVGCD PKADSTRLIL
60 70 80 90 100
HSKAQNTIME MAAEAGTVED LELEDVLKAG YGGVKCVESG GPEPGVGCAG
110 120 130 140 150
RGVITAINFL EEEGAYEDDL DFVFYDVLGD VVCGGFAMPI RENKAQEIYI
160 170 180 190 200
VCSGEMMAMY AANNISKGIV KYANSGSVRL GGLICNSRNT DREDELIIAL
210 220 230 240 250
ANKLGTQMIH FVPRDNVVQR AEIRRMTVIE YDPKAKQADE YRALARKVVD
260 270 280 290
NKLLVIPNPI TMDELEELLM EFGIMEVEDE SIVGKTAEEV
Length:290
Mass (Da):31,516
Last modified:January 23, 2007 - v2
Checksum:iC36EFC0D9A27F64D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145A → P in AAA22142 (PubMed:3863780).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20568 Genomic DNA. Translation: AAA64709.1.
M11579 Genomic DNA. Translation: AAA22142.1.
X06886 Genomic DNA. Translation: CAA30003.1.
PIRiA94666. NIAVF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20568 Genomic DNA. Translation: AAA64709.1.
M11579 Genomic DNA. Translation: AAA22142.1.
X06886 Genomic DNA. Translation: CAA30003.1.
PIRiA94666. NIAVF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DE0X-ray2.40A/B2-290[»]
1FP6X-ray2.15A/B/C/D2-290[»]
1G1MX-ray2.25A/B2-290[»]
1G20X-ray2.20E/F/G/H1-290[»]
1G21X-ray3.00E/F/G/H1-290[»]
1G5PX-ray2.20A/B2-290[»]
1M1YX-ray3.20E/F/G/H/M/N/O/P2-290[»]
1M34X-ray2.30E/F/G/H/M/N/O/P2-290[»]
1N2CX-ray3.00E/F/G/H2-290[»]
1NIPX-ray2.90A/B2-290[»]
1RW4X-ray2.50A2-273[»]
1XCPX-ray3.20A/B/C/D2-290[»]
1XD8X-ray2.70A/B2-290[»]
1XD9X-ray2.80A/B2-290[»]
1XDBX-ray2.80A/B2-290[»]
2AFHX-ray2.10E/F2-290[»]
2AFIX-ray3.10E/F/G/H/M/N/O/P2-290[»]
2C8VX-ray2.50A2-290[»]
2NIPX-ray2.20A/B2-290[»]
4WZAX-ray1.90E/F/G/H2-277[»]
4WZBX-ray2.30E/F/G/H2-273[»]
ProteinModelPortaliP00459.
SMRiP00459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322710.Avin_01380.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105DSM. Bacteria.
COG1348. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19495.
BRENDAi1.18.6.1. 49.

Miscellaneous databases

EvolutionaryTraceiP00459.

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 nameiNIFH1_AZOVI
AccessioniPrimary (citable) accession number: P00459
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This subunit is associated with the molybdenum-iron nitrogenase component 2.

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.