Nitrogenase molybdenum-iron protein alpha chain - Rhizobium sp. (strain NGR234)

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P19066 (NIFD_RHISN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nitrogenase molybdenum-iron protein alpha chain
EC=1.18.6.1

Alternative name(s):
Dinitrogenase
Nitrogenase component I

Gene names

Name:	nifD1
Ordered Locus Names:	NGR_a01120
ORF Names:	y4vL
AND
Name:	nifD2
Ordered Locus Names:	NGR_a00880
ORF Names:	y4xB

Encoded on

Plasmid sym pNGR234a

Organism

Rhizobium sp. (strain NGR234) [Complete proteome] [HAMAP]

Taxonomic identifier

394 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium ›

Protein attributes

Sequence length	504 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
Catalytic activity	8 reduced ferredoxin + 8 H⁺ + N₂ + 16 ATP + 16 H₂O = 8 oxidized ferredoxin + H₂ + 2 NH₃ + 16 ADP + 16 phosphate.
Cofactor	Binds 1 8Fe-7S cluster per heterodimer By similarity. Binds 1 7Fe-Mo-9S-X-homocitryl cluster per subunit. The identity of the X atom is not known, possibly carbon or oxygen By similarity.
Subunit structure	Tetramer of two alpha and two beta chains. Forms complex with the iron protein (nitrogenase component 2).
Sequence similarities	Belongs to the NifD/NifK/NifE/NifN family.

Ontologies

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 504

504

Nitrogenase molybdenum-iron protein alpha chain

PRO_0000153079

Sites

Metal binding

Iron-sulfur (8Fe-7S); shared with beta chain By similarity

Metal binding

Iron-sulfur (8Fe-7S); shared with beta chain By similarity

Metal binding

164

Iron-sulfur (8Fe-7S); shared with beta chain By similarity

Metal binding

287

Molybdenum-iron-sulfur (7Fe-Mo-9S-X-homocitryl) By similarity

Metal binding

454

Molybdenum-iron-sulfur (7Fe-Mo-9S-X-homocitryl); via pros nitrogen By similarity

Experimental info

Sequence conflict

201

Q → K in AAA26328. Ref.3

Sequence conflict

303

A → G in AAA26328. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P19066 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: D3BE3291A9D276DC
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FASTA

504

56,944

        10         20         30         40         50         60 
MSLDYENDSA LHQELITQVL SQYPHKAAKR RQKHLSVASD REAVGEEGET LSECDVKSNI 

        70         80         90        100        110        120 
KSIPGVMTIR GCAYAGSKGV VWGPVKDMVH ISHGPVGCGQ YSWSQRRNYY VGTTGVDTFV 

       130        140        150        160        170        180 
TMQFTSDFQE KDIVFGGDKK LEQVIDEIEE LFPLNNGITI QSECPIGLIG DDIEAVSRKK 

       190        200        210        220        230        240 
AAEHETTIVP VRCEGFRGVS QSLGHHIAND AIRDWVFDKA DGKTDVEFET GPYDVNVIGD 

       250        260        270        280        290        300 
YNIGGDAWAS RILLEEIGLR VVGNWSGDAT LAEVERAPRA KLNLIHCYRS MNYICRHMEE 

       310        320        330        340        350        360 
RYAIPWMEYN FFGPSQIEAS LRKIARHFGP TIEERAERVI AKYRPLVDAV IDKYWPRLQG 

       370        380        390        400        410        420 
KRVMLYVGGL RPRHVITAYE DLGMQIVGTG YEFAHNDDYQ RTGHYVKTGT LIYDDATSYE 

       430        440        450        460        470        480 
LDTFIERIRP DLVGSGIKEK YPVQKMGIPF RQMHSWDYSG PYHGYDGFAI FARDMDLAIN 

       490        500 
NPVWDLYDAP WKKMTVPTAA VAAE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular basis of symbiosis between Rhizobium and legumes." Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A., Perret X. Nature 387:394-401(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NGR234.
[2]	"Rhizobium sp. strain NGR234 possesses a remarkable number of secretion systems." Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A., Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., Broughton W.J., Perret X., Strittmatter A.W., Streit W.R. Appl. Environ. Microbiol. 75:4035-4045(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NGR234.
[3]	"Structural and functional analysis of nitrogenase genes from the broad-host-range Rhizobium strain ANU240." Badenoch-Jones J., Holton T.A., Morrison C.M., Scott K.F., Shine J. Gene 77:141-153(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16 AND 199-393. Strain: ANU 240.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00090 Genomic DNA. Translation: AAB91900.1. U00090 Genomic DNA. Translation: AAB91924.1. M26961 Genomic DNA. Translation: AAA26330.1. M26962 Genomic DNA. Translation: AAA26328.1.
PIR	PS0045. T10829.
RefSeq	NP_444113.1. NC_000914.2. NP_444137.1. NC_000914.2.
3D structure databases
ProteinModelPortal	P19066.
SMR	P19066. Positions 13-492.
ModBase	Search...
Protein-protein interaction databases
STRING	394.NGR_a01120.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB91900; AAB91900; NGR_a01120. AAB91924; AAB91924; NGR_a00880.
GeneID	962482. 962502.
KEGG	rhi:NGR_a00880. rhi:NGR_a01120.
PATRIC	32300883. VBIRhiSp122450_0077.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2710.
HOGENOM	HOG000005528.
KO	K02586.
OMA	LTRRNQT.
ProtClustDB	CLSK864414.
Enzyme and pathway databases
BioCyc	SFRE394:GBYN-6139-MONOMER. SFRE394:GBYN-6163-MONOMER.
Family and domain databases
InterPro	IPR000510. Nase/OxRdtase_comp1. IPR010143. Nase_comp1_asu. IPR000318. Nase_comp1_CS. IPR005972. Nase_Mo-Fe_asu. [Graphical view]
Pfam	PF00148. Oxidored_nitro. 1 hit. [Graphical view]
TIGRFAMs	TIGR01862. N2-ase-Ialpha. 1 hit. TIGR01282. nifD. 1 hit.
PROSITE	PS00699. NITROGENASE_1_1. 1 hit. PS00090. NITROGENASE_1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NIFD_RHISN

Accession

Primary (citable) accession number: P19066

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Rhizobium plasmid pNGR234a

Rhizobium plasmid pNGR234a: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents