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Protein

Nitrogen fixation regulatory protein

Gene

nifL

Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Required for the inhibition of NifA activity in response to oxygen and low level of fixed nitrogen.

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Cofactori

Redox potential

E0 is -226 mV.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. flavin adenine dinucleotide binding Source: InterPro
  3. phosphorelay sensor kinase activity Source: InterPro

GO - Biological processi

  1. nitrogen fixation Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: CACAO
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nitrogen fixation, Transcription, Transcription regulation, Two-component regulatory system

Keywords - Ligandi

ATP-binding, FAD, Flavoprotein, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogen fixation regulatory protein (EC:2.7.13.3)
Gene namesi
Name:nifL
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519Nitrogen fixation regulatory proteinPRO_0000074815Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei305 – 3051Phosphohistidine; by autocatalysisPROSITE-ProRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

IntActiP30663. 1 interaction.
MINTiMINT-107527.

Structurei

Secondary structure

1
519
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3310Combined sources
Beta strandi35 – 417Combined sources
Beta strandi46 – 505Combined sources
Helixi52 – 587Combined sources
Helixi64 – 674Combined sources
Helixi70 – 734Combined sources
Helixi80 – 9112Combined sources
Beta strandi96 – 1038Combined sources
Beta strandi109 – 12012Combined sources
Beta strandi126 – 13510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GJ3X-ray1.04A/B21-140[»]
ProteinModelPortaliP30663.
SMRiP30663. Positions 22-140.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30663.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 9371PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 14855PACPROSITE-ProRule annotationAdd
BLAST
Domaini151 – 21767PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini302 – 517216Histidine kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 1 PAC (PAS-associated C-terminal) domain.PROSITE-ProRule annotation
Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
InterProiIPR003594. HATPase_C.
IPR014285. N_fixation_neg-reg_NifL.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR013767. PAS_fold.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00989. PAS. 2 hits.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 2 hits.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR02938. nifL_nitrog. 1 hit.
TIGR00229. sensory_box. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30663-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTPANPTLSN EPQAPHAESD ELLPEIFRQT VEHAPIAISI TDLKANILYA
60 70 80 90 100
NRAFRTITGY GSEEVLGKNE SILSNGTTPR LVYQALWGRL AQKKPWSGVL
110 120 130 140 150
VNRRKDKTLY LAELTVAPVL NEAGETIYYL GMHRDTSELH ELEQRVNNQR
160 170 180 190 200
LMIEAVVNAA PAAMVVLDRQ HRVMLSNPSF CRLARDLVED GSSESLVALL
210 220 230 240 250
RENLAAPFET LENQGSAFSG KEISFDLGGR SPRWLSCHGR AIHIENEQAH
260 270 280 290 300
VFFAPTEERY LLLTINDISE LRQKQQDSRL NALKALMAEE ELLEGMRETF
310 320 330 340 350
NAAIHRLQGP VNLISAAMRM LERRLGDKAG NDPVLSAMRE ASTAGMEALE
360 370 380 390 400
NLSGSIPVRM AESKMPVNLN QLIREVITLC TDQLLAQGIV VDWQPALRLP
410 420 430 440 450
WVMGGESSQR SMIKHLVDNA IESMSQNQVS RRELFISTRV ENHLVRMEIT
460 470 480 490 500
DSGPGIPPDL VLKVFEPFFS TKPPHRVGRG MGLPVVQEIV AKHAGMVHVD
510
TDYREGCRIV VELPFSAST
Length:519
Mass (Da):57,827
Last modified:February 1, 1996 - v2
Checksum:iA40B1E76BD3723CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64832 Genomic DNA. Translation: CAA46044.1.
Y00554 Genomic DNA. Translation: CAA68632.1.
PIRiS19883.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64832 Genomic DNA. Translation: CAA46044.1.
Y00554 Genomic DNA. Translation: CAA68632.1.
PIRiS19883.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GJ3X-ray1.04A/B21-140[»]
ProteinModelPortaliP30663.
SMRiP30663. Positions 22-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP30663. 1 interaction.
MINTiMINT-107527.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP30663.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
InterProiIPR003594. HATPase_C.
IPR014285. N_fixation_neg-reg_NifL.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR013767. PAS_fold.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00989. PAS. 2 hits.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 2 hits.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR02938. nifL_nitrog. 1 hit.
TIGR00229. sensory_box. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequence and molecular analysis of the nifL gene of Azotobacter vinelandii."
    Blanco G., Drummond M., Woodley P., Kennedy C.
    Mol. Microbiol. 9:869-879(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW.
  2. "Nucleotide sequence and mutagenesis of the nifA gene from Azotobacter vinelandii."
    Bennet L.T., Cannon F., Dean D.R.
    Mol. Microbiol. 2:315-321(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 417-519.
    Strain: ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW.
  3. "Electron donation to the flavoprotein NifL, a redox-sensing transcriptional regulator."
    Macheroux P., Hill S., Austin S., Eydmann T., Jones T., Kim S.-O., Poole R., Dixon R.
    Biochem. J. 332:413-419(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "Azotobacter vinelandii NIFL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch."
    Hill S., Austin S., Eydmann T., Jones T., Dixon R.
    Proc. Natl. Acad. Sci. U.S.A. 93:2143-2148(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FAD AND ADP-BINDING.
  5. "The redox- and fixed nitrogen-responsive regulatory protein NIFL from Azotobacter vinelandii comprises discrete flavin and nucleotide-binding domains."
    Soederbaeck E., Reyes-Ramirez F., Eydmann T., Austin S., Hill S., Dixon R.
    Mol. Microbiol. 28:179-192(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FAD AND ADP-BINDING.
  6. "Crystallization and preliminary crystallographic data of the PAS domain of the NifL protein from Azotobacter vinelandii."
    Hefti M., Hendle J., Enroth C., Vervoort J., Tucker P.A.
    Acta Crystallogr. D 57:1895-1896(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.

Entry informationi

Entry nameiNIFL_AZOVI
AccessioniPrimary (citable) accession number: P30663
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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

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 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.