Q2JP78 (NIFH_SYNJB) 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:	CYB_0421

Organism

Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) [Complete proteome] [HAMAP]

Taxonomic identifier

321332 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus

Protein attributes

Sequence length	292 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.
Subunit structure	Homodimer By similarity.
Post-translational modification	The reversible ADP-ribosylation of Arg-99 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 – 292	292	Nitrogenase iron protein HAMAP-Rule MF_00533		PRO_1000211891
Regions
	Nucleotide binding	8 – 15	8	ATP Potential
Sites
	Metal binding	96	1	Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity
	Metal binding	130	1	Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity
Amino acid modifications
	Modified residue	99	1	ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2JP78 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 71FE840015DB6FDD	FASTA	292	31,978
	10 20 30 40 50 60 MRQIAFYGKG GIGKSTTCQN TVAGMAELGQ RIMIVGCDPK ADSTRLMLHC KAQTTVLHLA 70 80 90 100 110 120 AERGSVEDVE LEEVVLTGYR GVRCVESGGP EPGVGCAGRG IITAINFLEE NGAYEDLDFV 130 140 150 160 170 180 CYDVLGDVVC GGFAMPIREG KAQEIYIVCS GEMMAMYAAN NIARGVLKYA YSGGVRLGGL 190 200 210 220 230 240 ICNSRKVDRE IELIEALAEK LNTKMLHFIP RDNVVQHAEL RRMTVIEYSP DCNQADEYRA 250 260 270 280 290 LAKKIINNTD LRIPTPISMD ELEQLLIEFG VLDDDQKIAH LIGKTEKELA PV

References

[1]

"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses." Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F. ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JA-2-3B'a(2-13).

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000240 Genomic DNA. Translation: ABD01417.1.
RefSeq	YP_476680.1. NC_007776.1.
3D structure databases
HSSP	HSSP built from PDB template 2C8V based on UniProtKB P00459.
ProteinModelPortal	Q2JP78.
SMR	Q2JP78. Positions 1-289.
ModBase	Search...
Protein-protein interaction databases
STRING	321332.CYB_0421.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD01417; ABD01417; CYB_0421.
GeneID	3900876.
KEGG	cyb:CYB_0421.
PATRIC	23803130. VBISynSp29577_0431.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1348.
HOGENOM	HOG000228826.
KO	K02588.
OMA	CTESGGP.
ProtClustDB	CLSK750508.
Family and domain databases
HAMAP	MF_00533. NifH.
InterPro	IPR000392. Nitogenase_NifH/Reductase_ChlL. IPR005977. Nitrogenase_Fe_NifH. [Graphical view]
Pfam	PF00142. Fer4_NifH. 1 hit. [Graphical view]
PIRSF	PIRSF000363. Nitrogenase_iron. 1 hit.
PRINTS	PR00091. NITROGNASEII.
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_SYNJB

Accession

Primary (citable) accession number: Q2JP78

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program