ID NIFL_AZOVI Reviewed; 519 AA. AC P30663; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 02-SEP-2026, entry version 141. DE RecName: Full=Nitrogen fixation regulatory protein; DE EC=2.7.13.3; GN Name=nifL; OS Azotobacter vinelandii. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW; RX PubMed=8231815; DOI=10.1111/j.1365-2958.1993.tb01745.x; RA Blanco G., Drummond M., Woodley P., Kennedy C.; RT "Sequence and molecular analysis of the nifL gene of Azotobacter RT vinelandii."; RL Mol. Microbiol. 9:869-879(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 417-519. RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW; RX PubMed=2840552; DOI=10.1111/j.1365-2958.1988.tb00034.x; RA Bennet L.T., Cannon F., Dean D.R.; RT "Nucleotide sequence and mutagenesis of the nifA gene from Azotobacter RT vinelandii."; RL Mol. Microbiol. 2:315-321(1988). RN [3] RP CHARACTERIZATION. RX PubMed=9601070; DOI=10.1042/bj3320413; RA Macheroux P., Hill S., Austin S., Eydmann T., Jones T., Kim S.-O., RA Poole R., Dixon R.; RT "Electron donation to the flavoprotein NifL, a redox-sensing RT transcriptional regulator."; RL Biochem. J. 332:413-419(1998). RN [4] RP FAD AND ADP-BINDING. RX PubMed=8700899; DOI=10.1073/pnas.93.5.2143; RA Hill S., Austin S., Eydmann T., Jones T., Dixon R.; RT "Azotobacter vinelandii NIFL is a flavoprotein that modulates RT transcriptional activation of nitrogen-fixation genes via a redox-sensitive RT switch."; RL Proc. Natl. Acad. Sci. U.S.A. 93:2143-2148(1996). RN [5] RP FAD AND ADP-BINDING. RX PubMed=9593306; DOI=10.1046/j.1365-2958.1998.00788.x; RA Soederbaeck E., Reyes-Ramirez F., Eydmann T., Austin S., Hill S., Dixon R.; RT "The redox- and fixed nitrogen-responsive regulatory protein NIFL from RT Azotobacter vinelandii comprises discrete flavin and nucleotide-binding RT domains."; RL Mol. Microbiol. 28:179-192(1998). RN [6] RP CRYSTALLIZATION. RX PubMed=11717509; DOI=10.1107/s0907444901015657; RA Hefti M., Hendle J., Enroth C., Vervoort J., Tucker P.A.; RT "Crystallization and preliminary crystallographic data of the PAS domain of RT the NifL protein from Azotobacter vinelandii."; RL Acta Crystallogr. D 57:1895-1896(2001). CC -!- FUNCTION: Required for the inhibition of NifA activity in response to CC oxygen and low level of fixed nitrogen. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L- CC histidine.; EC=2.7.13.3; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Redox potential: CC E(0) is -226 mV.; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X64832; CAA46044.1; -; Genomic_DNA. DR EMBL; Y00554; CAA68632.1; -; Genomic_DNA. DR PIR; S19883; S19883. DR PDB; 2GJ3; X-ray; 1.04 A; A/B=21-140. DR AlphaFoldDB; P30663; -. DR SASBDB; P30663; -. DR SMR; P30663; -. DR IntAct; P30663; 1. DR EvolutionaryTrace; P30663; -. DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:CACAO. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd00130; PAS; 2. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 2. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR003594; HATPase_dom. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR014285; N_fixation_neg-reg_NifL. DR InterPro; IPR001610; PAC. DR InterPro; IPR000014; PAS. DR InterPro; IPR000700; PAS-assoc_C. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR013767; PAS_fold. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR NCBIfam; TIGR02938; nifL_nitrog; 1. DR NCBIfam; TIGR00229; sensory_box; 1. DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1. DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00989; PAS; 2. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 2. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50113; PAC; 1. DR PROSITE; PS50112; PAS; 1. DR PDBsum; 2GJ3; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; FAD; Flavoprotein; Kinase; Nitrogen fixation; KW Nucleotide-binding; Phosphoprotein; Repeat; Transcription; KW Transcription regulation; Transferase; Two-component regulatory system. FT CHAIN 1..519 FT /note="Nitrogen fixation regulatory protein" FT /id="PRO_0000074815" FT DOMAIN 23..93 FT /note="PAS 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140" FT DOMAIN 94..148 FT /note="PAC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141" FT DOMAIN 151..217 FT /note="PAS 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140" FT DOMAIN 302..517 FT /note="Histidine kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107" FT MOD_RES 305 FT /note="Phosphohistidine; by autocatalysis" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107" FT HELIX 24..33 FT /evidence="ECO:0007829|PDB:2GJ3" FT STRAND 35..41 FT /evidence="ECO:0007829|PDB:2GJ3" FT STRAND 46..50 FT /evidence="ECO:0007829|PDB:2GJ3" FT HELIX 52..58 FT /evidence="ECO:0007829|PDB:2GJ3" FT HELIX 64..67 FT /evidence="ECO:0007829|PDB:2GJ3" FT HELIX 70..73 FT /evidence="ECO:0007829|PDB:2GJ3" FT HELIX 80..91 FT /evidence="ECO:0007829|PDB:2GJ3" FT STRAND 96..103 FT /evidence="ECO:0007829|PDB:2GJ3" FT STRAND 109..120 FT /evidence="ECO:0007829|PDB:2GJ3" FT STRAND 126..135 FT /evidence="ECO:0007829|PDB:2GJ3" SQ SEQUENCE 519 AA; 57827 MW; A40B1E76BD3723CB CRC64; MTPANPTLSN EPQAPHAESD ELLPEIFRQT VEHAPIAISI TDLKANILYA NRAFRTITGY GSEEVLGKNE SILSNGTTPR LVYQALWGRL AQKKPWSGVL VNRRKDKTLY LAELTVAPVL NEAGETIYYL GMHRDTSELH ELEQRVNNQR LMIEAVVNAA PAAMVVLDRQ HRVMLSNPSF CRLARDLVED GSSESLVALL RENLAAPFET LENQGSAFSG KEISFDLGGR SPRWLSCHGR AIHIENEQAH VFFAPTEERY LLLTINDISE LRQKQQDSRL NALKALMAEE ELLEGMRETF NAAIHRLQGP VNLISAAMRM LERRLGDKAG NDPVLSAMRE ASTAGMEALE NLSGSIPVRM AESKMPVNLN QLIREVITLC TDQLLAQGIV VDWQPALRLP WVMGGESSQR SMIKHLVDNA IESMSQNQVS RRELFISTRV ENHLVRMEIT DSGPGIPPDL VLKVFEPFFS TKPPHRVGRG MGLPVVQEIV AKHAGMVHVD TDYREGCRIV VELPFSAST //