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P07329

- NIFK_AZOVI

UniProt

P07329 - NIFK_AZOVI

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Protein

Nitrogenase molybdenum-iron protein beta chain

Gene

nifK

Organism
Azotobacter vinelandii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.

Catalytic activityi

8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate.

Cofactori

[8Fe-7S] clusterNote: Binds 1 [8Fe-7S] cluster per heterodimer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi70 – 701Iron-sulfur (8Fe-7S); shared with alpha chain
Metal bindingi95 – 951Iron-sulfur (8Fe-7S); shared with alpha chain
Metal bindingi153 – 1531Iron-sulfur (8Fe-7S); shared with alpha chain
Metal bindingi188 – 1881Iron-sulfur (8Fe-7S); shared with alpha chain

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. carbonyl sulfide nitrogenase activity Source: UniProtKB-EC
  3. iron-sulfur cluster binding Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. nitrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. nitrogen fixation Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrogen fixation

Keywords - Ligandi

ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogenase molybdenum-iron protein beta chain (EC:1.18.6.1)
Alternative name(s):
Dinitrogenase
Nitrogenase component I
Gene namesi
Name:nifK
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Subcellular locationi

GO - Cellular componenti

  1. molybdenum-iron nitrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 523522Nitrogenase molybdenum-iron protein beta chainPRO_0000153091Add
BLAST

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains. Forms complex with the iron protein (nitrogenase component 2).

Protein-protein interaction databases

MINTiMINT-1508555.

Structurei

Secondary structure

1
523
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Helixi11 – 144Combined sources
Helixi18 – 3114Combined sources
Helixi37 – 4610Combined sources
Helixi50 – 578Combined sources
Beta strandi63 – 653Combined sources
Helixi71 – 8010Combined sources
Beta strandi85 – 917Combined sources
Helixi93 – 10715Combined sources
Beta strandi114 – 1174Combined sources
Helixi120 – 1234Combined sources
Helixi128 – 14215Combined sources
Beta strandi145 – 1517Combined sources
Helixi153 – 1586Combined sources
Helixi162 – 17110Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi188 – 1914Combined sources
Helixi193 – 20917Combined sources
Helixi210 – 2156Combined sources
Turni218 – 2214Combined sources
Beta strandi224 – 2274Combined sources
Helixi234 – 24613Combined sources
Beta strandi251 – 2555Combined sources
Turni258 – 2614Combined sources
Beta strandi266 – 2683Combined sources
Helixi278 – 2836Combined sources
Helixi284 – 2863Combined sources
Beta strandi287 – 2948Combined sources
Helixi295 – 2973Combined sources
Helixi299 – 3079Combined sources
Helixi321 – 33616Combined sources
Helixi342 – 36221Combined sources
Beta strandi366 – 3705Combined sources
Helixi373 – 38513Combined sources
Beta strandi389 – 3957Combined sources
Helixi400 – 41112Combined sources
Helixi414 – 4163Combined sources
Beta strandi420 – 4245Combined sources
Helixi427 – 43610Combined sources
Beta strandi440 – 4445Combined sources
Helixi448 – 45811Combined sources
Helixi460 – 4623Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi475 – 4784Combined sources
Helixi479 – 4813Combined sources
Helixi486 – 50823Combined sources
Turni512 – 5154Combined sources
Helixi516 – 5183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4TKUX-ray1.43B/D1-523[»]
4TKVX-ray1.50B/D1-523[»]
ProteinModelPortaliP07329.
SMRiP07329. Positions 2-523.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07329.

Family & Domainsi

Sequence similaritiesi

Belongs to the NifD/NifK/NifE/NifN family.Curated

Family and domain databases

InterProiIPR000510. Nase/OxRdtase_comp1.
IPR000318. Nase_comp1_CS.
IPR005976. Nase_Mo-Fe_CF_bsu.
IPR024564. Nase_Mo-Fe_CF_bsu_N.
[Graphical view]
PfamiPF11844. DUF3364. 1 hit.
PF00148. Oxidored_nitro. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01286. nifK. 1 hit.
PROSITEiPS00699. NITROGENASE_1_1. 1 hit.
PS00090. NITROGENASE_1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07329-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQQVDKIKA SYPLFLDQDY KDMLAKKRDG FEEKYPQDKI DEVFQWTTTK
60 70 80 90 100
EYQELNFQRE ALTVNPAKAC QPLGAVLCAL GFEKTMPYVH GSQGCVAYFR
110 120 130 140 150
SYFNRHFREP VSCVSDSMTE DAAVFGGQQN MKDGLQNCKA TYKPDMIAVS
160 170 180 190 200
TTCMAEVIGD DLNAFINNSK KEGFIPDEFP VPFAHTPSFV GSHVTGWDNM
210 220 230 240 250
FEGIARYFTL KSMDDKVVGS NKKINIVPGF ETYLGNFRVI KRMLSEMGVG
260 270 280 290 300
YSLLSDPEEV LDTPADGQFR MYAGGTTQEE MKDAPNALNT VLLQPWHLEK
310 320 330 340 350
TKKFVEGTWK HEVPKLNIPM GLDWTDEFLM KVSEISGQPI PASLTKERGR
360 370 380 390 400
LVDMMTDSHT WLHGKRFALW GDPDFVMGLV KFLLELGCEP VHILCHNGNK
410 420 430 440 450
RWKKAVDAIL AASPYGKNAT VYIGKDLWHL RSLVFTDKPD FMIGNSYGKF
460 470 480 490 500
IQRDTLHKGK EFEVPLIRIG FPIFDRHHLH RSTTLGYEGA MQILTTLVNS
510 520
ILERLDEETR GMQATDYNHD LVR
Length:523
Mass (Da):59,460
Last modified:January 23, 2007 - v3
Checksum:iB6ECD633A24998F2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031F → L in AAA22144. (PubMed:3863780)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20568 Genomic DNA. Translation: AAA64711.1.
M11579 Genomic DNA. Translation: AAA22144.1.
PIRiB43049. NIAVMB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20568 Genomic DNA. Translation: AAA64711.1 .
M11579 Genomic DNA. Translation: AAA22144.1 .
PIRi B43049. NIAVMB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FP4 X-ray 2.50 B/D 1-523 [» ]
1G20 X-ray 2.20 B/D 1-523 [» ]
1G21 X-ray 3.00 B/D 1-523 [» ]
1L5H X-ray 2.30 B 2-523 [» ]
1M1N X-ray 1.16 B/D/F/H 2-523 [» ]
1M1Y X-ray 3.20 B/D/J/L 2-523 [» ]
1M34 X-ray 2.30 B/D/J/L 2-523 [» ]
1N2C X-ray 3.00 B/D 2-523 [» ]
2AFH X-ray 2.10 B/D 2-523 [» ]
2AFI X-ray 3.10 B/D/J/L 2-523 [» ]
2AFK X-ray 2.30 B/D 2-523 [» ]
2MIN X-ray 2.03 B/D 2-523 [» ]
3K1A X-ray 2.23 B/D 2-523 [» ]
3MIN X-ray 2.03 B/D 2-523 [» ]
3U7Q X-ray 1.00 B/D 1-523 [» ]
4ND8 X-ray 2.00 B/D 1-523 [» ]
4TKU X-ray 1.43 B/D 1-523 [» ]
4TKV X-ray 1.50 B/D 1-523 [» ]
ProteinModelPortali P07329.
SMRi P07329. Positions 2-523.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1508555.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P07329.

Family and domain databases

InterProi IPR000510. Nase/OxRdtase_comp1.
IPR000318. Nase_comp1_CS.
IPR005976. Nase_Mo-Fe_CF_bsu.
IPR024564. Nase_Mo-Fe_CF_bsu_N.
[Graphical view ]
Pfami PF11844. DUF3364. 1 hit.
PF00148. Oxidored_nitro. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01286. nifK. 1 hit.
PROSITEi PS00699. NITROGENASE_1_1. 1 hit.
PS00090. NITROGENASE_1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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).

Entry informationi

Entry nameiNIFK_AZOVI
AccessioniPrimary (citable) accession number: P07329
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3