Nitrogen fixation regulatory protein - Azotobacter vinelandii

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P30663 (NIFL_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 92. 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:
Nitrogen fixation regulatory protein
EC=2.7.13.3

Gene names

Name:

nifL

Organism

Azotobacter vinelandii

Taxonomic identifier

354 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the inhibition of NifA activity in response to oxygen and low level of fixed nitrogen.
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Cofactor	FAD.
Sequence similarities	Contains 1 histidine kinase domain. Contains 1 PAC (PAS-associated C-terminal) domain. Contains 2 PAS (PER-ARNT-SIM) domains.
Biophysicochemical properties	Redox potential: E₀ is -226 mV.

Ontologies

Keywords
Biological process	Nitrogen fixation Transcription Transcription regulation Two-component regulatory system
Domain	Repeat
Ligand	ATP-binding FAD Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	nitrogen fixation Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro phosphorelay sensor kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 519

519

Nitrogen fixation regulatory protein

PRO_0000074815

Regions

Domain

23 – 93

PAS 1

Domain

94 – 148

PAC

Domain

151 – 217

PAS 2

Domain

302 – 517

216

Histidine kinase

Amino acid modifications

Modified residue

305

Phosphohistidine; by autocatalysis By similarity

Secondary structure

519

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P30663 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: A40B1E76BD3723CB
Show »

FASTA

519

57,827

        10         20         30         40         50         60 
MTPANPTLSN EPQAPHAESD ELLPEIFRQT VEHAPIAISI TDLKANILYA NRAFRTITGY 

        70         80         90        100        110        120 
GSEEVLGKNE SILSNGTTPR LVYQALWGRL AQKKPWSGVL VNRRKDKTLY LAELTVAPVL 

       130        140        150        160        170        180 
NEAGETIYYL GMHRDTSELH ELEQRVNNQR LMIEAVVNAA PAAMVVLDRQ HRVMLSNPSF 

       190        200        210        220        230        240 
CRLARDLVED GSSESLVALL RENLAAPFET LENQGSAFSG KEISFDLGGR SPRWLSCHGR 

       250        260        270        280        290        300 
AIHIENEQAH VFFAPTEERY LLLTINDISE LRQKQQDSRL NALKALMAEE ELLEGMRETF 

       310        320        330        340        350        360 
NAAIHRLQGP VNLISAAMRM LERRLGDKAG NDPVLSAMRE ASTAGMEALE NLSGSIPVRM 

       370        380        390        400        410        420 
AESKMPVNLN QLIREVITLC TDQLLAQGIV VDWQPALRLP WVMGGESSQR SMIKHLVDNA 

       430        440        450        460        470        480 
IESMSQNQVS RRELFISTRV ENHLVRMEIT DSGPGIPPDL VLKVFEPFFS TKPPHRVGRG 

       490        500        510 
MGLPVVQEIV AKHAGMVHVD TDYREGCRIV VELPFSAST

« Hide

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X64832 Genomic DNA. Translation: CAA46044.1.
Y00554 Genomic DNA. Translation: CAA68632.1.

PIR

S19883.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GJ3	X-ray	1.04	A/B	21-140	[»]

ProteinModelPortal

P30663.

SMR

P30663. Positions 22-140.

ModBase

Search...

Protein-protein interaction databases

IntAct

P30663. 1 interaction.

MINT

MINT-107527.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.30.565.10. 1 hit.

InterPro

IPR003594. HATPase_ATP-bd.
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]

Pfam

PF02518. HATPase_c. 1 hit.
PF00989. PAS. 2 hits.
[Graphical view]

PRINTS

PR00344. BCTRLSENSOR.

SMART

SM00387. HATPase_c. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF55785. SSF55785. 2 hits.

TIGRFAMs

TIGR02938. nifL_nitrog. 1 hit.
TIGR00229. sensory_box. 1 hit.

PROSITE

PS50109. HIS_KIN. 1 hit.
PS50113. PAC. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P30663.

Entry information

Entry name

NIFL_AZOVI

Accession

Primary (citable) accession number: P30663

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	February 1, 1996
Last modified:	May 29, 2013
This is version 92 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Family and domain databases

Other

Entry information

Relevant documents