Q2J1I1 (NIFH_RHOP2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nitrogenase iron protein
EC=1.18.6.1

Alternative name(s):
Nitrogenase Fe protein
Nitrogenase component II
Nitrogenase reductase

Gene names

Name:	nifH
Ordered Locus Names:	RPB_0969

Organism

Rhodopseudomonas palustris (strain HaA2) [Complete proteome] [HAMAP]

Taxonomic identifier

316058 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas › Rhodopseudomonas palustris

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 By similarity. HAMAP-Rule MF_00533
Catalytic activity	8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate. HAMAP-Rule MF_00533
Cofactor	Binds 1 4Fe-4S cluster per dimer By similarity. HAMAP-Rule MF_00533
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_00533
Post-translational modification	The reversible ADP-ribosylation of Arg-102 inactivates the nitrogenase reductase and regulates nitrogenase activity By similarity. HAMAP-Rule MF_00533
Sequence similarities	Belongs to the NifH/BchL/ChlL family.

Ontologies

Keywords
Biological process	Nitrogen fixation
Ligand	4Fe-4S ATP-binding Iron Iron-sulfur Metal-binding Nucleotide-binding
Molecular function	Oxidoreductase
PTM	ADP-ribosylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	nitrogen fixation Inferred from electronic annotation. Source: HAMAP
Cellular_component	molybdenum-iron nitrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW ATP binding Inferred from electronic annotation. Source: HAMAP carbonyl sulfide nitrogenase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 299	299	Nitrogenase iron protein HAMAP-Rule MF_00533		PRO_1000211883
Regions
	Nucleotide binding	11 – 18	8	ATP Potential
Sites
	Metal binding	99	1	Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity
	Metal binding	133	1	Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity
Amino acid modifications
	Modified residue	102	1	ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2J1I1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 35204D3B3FEE0322	FASTA	299	31,960
	10 20 30 40 50 60 MAALRQIAFY GKGGIGKSTT SQNTLAALVE LGQKILIVGC DPKADSTRLI LNTKMQDTVL 70 80 90 100 110 120 SLAAEAGSVE DLELEDVMKI GYKGIKCTEA GGPEPGVGCA GRGVITAINF LEENGAYEDV 130 140 150 160 170 180 DYVSYDVLGD VVCGGFAMPI RENKAQEIYI VMSGEMMALY AANNIAKGIL KYASSGGVRL 190 200 210 220 230 240 GGLICNERQT DRELDLAEAL AARLNSKLIH FVPRANIVQH AELRRQTVIE YAPDSQQAQE 250 260 270 280 290 YRQLANKIHA NSGNGTIPTP ITMEELEGML LDFGIMKTDE QALAELAEKE AAKAAAATA

References

[1]

"Complete sequence of Rhodopseudomonas palustris HaA2." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A. , Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HaA2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000250 Genomic DNA. Translation: ABD05679.1.
RefSeq	YP_484590.1. NC_007778.1.
3D structure databases
ProteinModelPortal	Q2J1I1.
ModBase	Search...
Protein-protein interaction databases
STRING	316058.RPB_0969.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD05679; ABD05679; RPB_0969.
GeneID	3909324.
KEGG	rpb:RPB_0969.
PATRIC	23296435. VBIRhoPal125544_1013.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1348.
HOGENOM	HOG000228826.
KO	K02588.
OMA	CTESGGP.
ProtClustDB	PRK13234.
Enzyme and pathway databases
BioCyc	RPAL316058:GHF1-984-MONOMER.
Family and domain databases
HAMAP	MF_00533. NifH.
InterPro	IPR000392. Nitogenase_NifH/Reductase_ChlL. IPR005977. Nitrogenase_Fe_NifH. IPR027417. P-loop_NTPase. [Graphical view]
Pfam	PF00142. Fer4_NifH. 1 hit. [Graphical view]
PIRSF	PIRSF000363. Nitrogenase_iron. 1 hit.
PRINTS	PR00091. NITROGNASEII.
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR01287. nifH. 1 hit.
PROSITE	PS00746. NIFH_FRXC_1. 1 hit. PS00692. NIFH_FRXC_2. 1 hit. PS51026. NIFH_FRXC_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NIFH_RHOP2

Accession

Primary (citable) accession number: Q2J1I1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	March 7, 2006
Last modified:	May 29, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program