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Protein

Nitrogenase molybdenum-iron protein beta chain

Gene

nifK

Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 5 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.

Enzyme regulationi

Nitrogenase holoenzyme is subject to "conformational protection" by FeSII; under oxidizing conditions FeSII binds to the holoenzyme and reversibly protects it from oxidation (PubMed:7830548).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi70Iron-sulfur (8Fe-7S); shared with alpha chain1
Metal bindingi95Iron-sulfur (8Fe-7S); shared with alpha chain1
Metal bindingi153Iron-sulfur (8Fe-7S); shared with alpha chain1
Metal bindingi188Iron-sulfur (8Fe-7S); shared with alpha chain1

GO - Molecular functioni

GO - Biological processi

  • 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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19494.

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

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001530912 – 523Nitrogenase molybdenum-iron protein beta chainAdd BLAST522

Expressioni

Inductioni

Constitutively expressed during log and stationary phase in sucrose-limited cultures, its levels decrease during stationary phase (at protein level).1 Publication

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.
STRINGi322710.Avin_01400.

Structurei

Secondary structure

1523
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Helixi11 – 14Combined sources4
Helixi18 – 31Combined sources14
Helixi37 – 46Combined sources10
Helixi50 – 57Combined sources8
Beta strandi63 – 65Combined sources3
Helixi71 – 80Combined sources10
Beta strandi85 – 91Combined sources7
Helixi93 – 107Combined sources15
Beta strandi114 – 117Combined sources4
Helixi120 – 123Combined sources4
Helixi128 – 142Combined sources15
Beta strandi145 – 151Combined sources7
Helixi153 – 158Combined sources6
Helixi162 – 171Combined sources10
Beta strandi177 – 179Combined sources3
Beta strandi188 – 191Combined sources4
Helixi193 – 209Combined sources17
Helixi210 – 215Combined sources6
Turni218 – 221Combined sources4
Beta strandi224 – 227Combined sources4
Helixi234 – 246Combined sources13
Beta strandi251 – 255Combined sources5
Turni258 – 261Combined sources4
Beta strandi266 – 268Combined sources3
Helixi278 – 283Combined sources6
Helixi284 – 286Combined sources3
Beta strandi287 – 294Combined sources8
Helixi295 – 297Combined sources3
Helixi299 – 307Combined sources9
Helixi321 – 336Combined sources16
Helixi342 – 362Combined sources21
Beta strandi366 – 370Combined sources5
Helixi373 – 385Combined sources13
Beta strandi389 – 395Combined sources7
Helixi400 – 411Combined sources12
Helixi414 – 416Combined sources3
Beta strandi420 – 424Combined sources5
Helixi427 – 436Combined sources10
Beta strandi440 – 444Combined sources5
Helixi448 – 458Combined sources11
Helixi460 – 462Combined sources3
Beta strandi466 – 468Combined sources3
Beta strandi475 – 478Combined sources4
Helixi479 – 481Combined sources3
Helixi486 – 508Combined sources23
Turni512 – 515Combined sources4
Helixi516 – 518Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
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[»]
4WNAX-ray2.00B/D1-523[»]
4WZAX-ray1.90B/D2-523[»]
4WZBX-ray2.30B/D2-523[»]
4XPIX-ray1.97B/D2-523[»]
5BVGX-ray1.60B/D1-523[»]
5BVHX-ray1.53B/D1-523[»]
5CX1X-ray1.75B/D/F/H/J/L/N/P1-523[»]
ProteinModelPortaliP07329.
SMRiP07329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07329.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CY9. Bacteria.
COG2710. LUCA.

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)DescriptionActionsGraphical viewLength
Sequence conflicti103F → L in AAA22144 (PubMed:3863780).Curated1

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.
PIRiB43049. NIAVMB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
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[»]
4WNAX-ray2.00B/D1-523[»]
4WZAX-ray1.90B/D2-523[»]
4WZBX-ray2.30B/D2-523[»]
4XPIX-ray1.97B/D2-523[»]
5BVGX-ray1.60B/D1-523[»]
5BVHX-ray1.53B/D1-523[»]
5CX1X-ray1.75B/D/F/H/J/L/N/P1-523[»]
ProteinModelPortaliP07329.
SMRiP07329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1508555.
STRINGi322710.Avin_01400.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CY9. Bacteria.
COG2710. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19494.

Miscellaneous databases

EvolutionaryTraceiP07329.

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]
ProtoNetiSearch...

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 2, 2016
This is version 110 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.