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P07329 (NIFK_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nitrogenase molybdenum-iron protein beta chain

EC=1.18.6.1
Alternative name(s):
Dinitrogenase
Nitrogenase component I
Gene names
Name:nifK
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 523522Nitrogenase molybdenum-iron protein beta chain
PRO_0000153091

Sites

Metal binding701Iron-sulfur (8Fe-7S); shared with alpha chain
Metal binding951Iron-sulfur (8Fe-7S); shared with alpha chain
Metal binding1531Iron-sulfur (8Fe-7S); shared with alpha chain
Metal binding1881Iron-sulfur (8Fe-7S); shared with alpha chain

Experimental info

Sequence conflict1031F → L in AAA22144. Ref.2

Secondary structure

........................................................................................... 523
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07329 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B6ECD633A24998F2

FASTA52359,460
        10         20         30         40         50         60 
MSQQVDKIKA SYPLFLDQDY KDMLAKKRDG FEEKYPQDKI DEVFQWTTTK EYQELNFQRE 

        70         80         90        100        110        120 
ALTVNPAKAC QPLGAVLCAL GFEKTMPYVH GSQGCVAYFR SYFNRHFREP VSCVSDSMTE 

       130        140        150        160        170        180 
DAAVFGGQQN MKDGLQNCKA TYKPDMIAVS TTCMAEVIGD DLNAFINNSK KEGFIPDEFP 

       190        200        210        220        230        240 
VPFAHTPSFV GSHVTGWDNM FEGIARYFTL KSMDDKVVGS NKKINIVPGF ETYLGNFRVI 

       250        260        270        280        290        300 
KRMLSEMGVG YSLLSDPEEV LDTPADGQFR MYAGGTTQEE MKDAPNALNT VLLQPWHLEK 

       310        320        330        340        350        360 
TKKFVEGTWK HEVPKLNIPM GLDWTDEFLM KVSEISGQPI PASLTKERGR LVDMMTDSHT 

       370        380        390        400        410        420 
WLHGKRFALW GDPDFVMGLV KFLLELGCEP VHILCHNGNK RWKKAVDAIL AASPYGKNAT 

       430        440        450        460        470        480 
VYIGKDLWHL RSLVFTDKPD FMIGNSYGKF IQRDTLHKGK EFEVPLIRIG FPIFDRHHLH 

       490        500        510        520 
RSTTLGYEGA MQILTTLVNS ILERLDEETR GMQATDYNHD LVR 

« Hide

References

[1]"Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii."
Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R.
J. Bacteriol. 171:1017-1027(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase structural gene cluster."
Brigle K.E., Newton W.E., Dean D.R.
Gene 37:37-44(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Isolation and partial characterization of two different subunits from the molybdenum-iron protein of Azotobacter vinelandii nitrogenase."
Lundell D.J., Howard J.B.
J. Biol. Chem. 253:3422-3426(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-20 AND 521-523.
[4]"Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii."
Kim J., Rees D.C.
Nature 360:553-560(1992)
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[5]"Structure of ADP x [AlF(4)](-)-stabilized nitrogenase complex and its implications for signal transduction."
Schindelin H., Kisker C., Schlessman J.L., Howard J.B., Rees D.C.
Nature 387:370-376(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[6]"Redox-dependent structural changes in the nitrogenase P-cluster."
Peters J.W., Stowell M.H.B., Soltis S.M., Finnegan M.G., Johnson M.K., Rees D.C.
Biochemistry 36:1181-1187(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[7]"MgATP-bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127Delta-Fe-protein and the MoFe-protein."
Chiu H.-J., Peters J.W., Lanzilotta W.N., Ryle M.J., Seefeldt L.C., Howard J.B., Rees D.C.
Biochemistry 40:641-650(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[8]"Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe protein."
Soerlie M., Christiansen J., Lemon B.J., Peters J.W., Dean D.R., Hales B.J.
Biochemistry 40:1540-1549(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLN-195.
[9]"Biochemical and structural characterization of the cross-linked complex of nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure."
Schmid B., Einsle O., Chiu H.J., Willing A., Yoshida M., Howard J.B., Rees D.C.
Biochemistry 41:15557-15565(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF CROSS-LINKED HETERODIMER WITH FE-PROTEIN.
[10]"Structure of a cofactor-deficient nitrogenase MoFe protein."
Schmid B., Ribbe M.W., Einsle O., Yoshida M., Thomas L.M., Dean D.R., Rees D.C., Burgess B.K.
Science 296:352-356(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[11]"Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor."
Einsle O., Tezcan F.A., Andrade S.L.A., Schmid B., Yoshida M., Howard J.B., Rees D.C.
Science 297:1696-1700(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20568 Genomic DNA. Translation: AAA64711.1.
M11579 Genomic DNA. Translation: AAA22144.1.
PIRNIAVMB. B43049.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FP4X-ray2.50B/D1-523[»]
1G20X-ray2.20B/D1-523[»]
1G21X-ray3.00B/D1-523[»]
1L5HX-ray2.30B2-523[»]
1M1NX-ray1.16B/D/F/H2-523[»]
1M1YX-ray3.20B/D/J/L2-523[»]
1M34X-ray2.30B/D/J/L2-523[»]
1N2CX-ray3.00B/D2-523[»]
2AFHX-ray2.10B/D2-523[»]
2AFIX-ray3.10B/D/J/L2-523[»]
2AFKX-ray2.30B/D2-523[»]
2MINX-ray2.03B/D2-523[»]
3K1AX-ray2.23B/D2-523[»]
3MINX-ray2.03B/D2-523[»]
3U7QX-ray1.00B/D1-523[»]
4ND8X-ray2.00B/D1-523[»]
ProteinModelPortalP07329.
SMRP07329. Positions 2-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1508555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000510. Nase/OxRdtase_comp1.
IPR000318. Nase_comp1_CS.
IPR005976. Nase_Mo-Fe_CF_bsu.
IPR024564. Nase_Mo-Fe_CF_bsu_N.
[Graphical view]
PfamPF11844. DUF3364. 1 hit.
PF00148. Oxidored_nitro. 1 hit.
[Graphical view]
TIGRFAMsTIGR01286. nifK. 1 hit.
PROSITEPS00699. NITROGENASE_1_1. 1 hit.
PS00090. NITROGENASE_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07329.

Entry information

Entry nameNIFK_AZOVI
AccessionPrimary (citable) accession number: P07329
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references