FLAV_AZOVI
ID FLAV_AZOVI Reviewed; 180 AA.
AC P00324;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Flavodoxin 2 {ECO:0000303|PubMed:8694750};
DE AltName: Full=AvFld 2 {ECO:0000303|PubMed:8694750};
DE AltName: Full=Flavodoxin II {ECO:0000303|PubMed:16131657};
GN Name=nifF {ECO:0000303|PubMed:8694750};
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC 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=2644218; DOI=10.1128/jb.171.2.1017-1027.1989;
RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S.,
RA Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT "Physical and genetic map of the major nif gene cluster from Azotobacter
RT vinelandii.";
RL J. Bacteriol. 171:1017-1027(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3121629; DOI=10.1016/s0021-9258(19)57311-2;
RA Bennett L., Jacobson M., Dean D.R.;
RT "Isolation, sequencing, and mutagenesis of the nifF gene encoding
RT flavodoxin from Azotobacter vinelandii.";
RL J. Biol. Chem. 263:1364-1369(1988).
RN [3]
RP PROTEIN SEQUENCE OF 2-180.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=889809; DOI=10.1021/bi00635a005;
RA Tanaka M., Haniu M., Yasunobu K.T., Yoch D.C.;
RT "Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter
RT vinelandii.";
RL Biochemistry 16:3525-3537(1977).
RN [4]
RP PROTEIN SEQUENCE OF 2-21, MASS SPECTROMETRY, FUNCTION, COFACTOR, INDUCTION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=OP / UW136;
RX PubMed=8694750; DOI=10.1042/bj3170103;
RA Gangeswaran R., Eady R.R.;
RT "Flavodoxin 1 of Azotobacter vinelandii: characterization and role in
RT electron donation to purified assimilatory nitrate reductase.";
RL Biochem. J. 317:103-108(1996).
RN [5]
RP STRUCTURE BY NMR.
RC STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / NBRC
RC 102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16;
RX PubMed=9521106; DOI=10.1002/pro.5560070210;
RA Steensma E., Nijman M.J.M., Bollen Y.J.M., de Jager P.A.,
RA van den Berg W.A.M., van Dongen W.M.A.M., van Mierlo C.P.M.;
RT "Apparent local stability of the secondary structure of Azotobacter
RT vinelandii holoflavodoxin II as probed by hydrogen exchange: implications
RT for redox potential regulation and flavodoxin folding.";
RL Protein Sci. 7:306-317(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT ALA-70 IN COMPLEX WITH
RP FMN, AND COFACTOR.
RC STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / NBRC
RC 102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16;
RX PubMed=16131657; DOI=10.1110/ps.051582605;
RA Alagaratnam S., van Pouderoyen G., Pijning T., Dijkstra B.W., Cavazzini D.,
RA Rossi G.L., Van Dongen W.M., van Mierlo C.P., van Berkel W.J.,
RA Canters G.W.;
RT "A crystallographic study of Cys69Ala flavodoxin II from Azotobacter
RT vinelandii: structural determinants of redox potential.";
RL Protein Sci. 14:2284-2295(2005).
CC -!- FUNCTION: Flavodoxins are low-potential electron donors to a number of
CC redox enzymes. NifF is the electron donor to nitrogenase, and is thus
CC implicated in nitrogen fixation. Does not function as an electron donor
CC to nitrite reductase. {ECO:0000269|PubMed:8694750}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:16131657, ECO:0000269|PubMed:8694750};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -493 mV. It is the mid-point potential of the
CC semiquinone/hydroquinone redox couple (SQ/HQ) of AvFld 2.
CC {ECO:0000269|PubMed:8694750};
CC -!- INDUCTION: Is the predominant flavodoxin expressed when A.vinelandii is
CC grown on N(2) as nitrogen source. Is also synthesized during growth on
CC nitrate, but in less abundance than AvFld 1.
CC {ECO:0000269|PubMed:8694750}.
CC -!- MASS SPECTROMETRY: Mass=19533; Mass_error=5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8694750};
CC -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR EMBL; M20568; AAA64735.1; -; Genomic_DNA.
DR EMBL; J03519; AAA22154.1; -; Genomic_DNA.
DR PIR; A29935; FXAVEP.
DR RefSeq; WP_012698862.1; NZ_FPKM01000020.1.
DR PDB; 1YOB; X-ray; 2.25 A; A/B=2-180.
DR PDB; 5K9B; X-ray; 1.17 A; A=1-180.
DR PDBsum; 1YOB; -.
DR PDBsum; 5K9B; -.
DR AlphaFoldDB; P00324; -.
DR BMRB; P00324; -.
DR SMR; P00324; -.
DR OMA; CENESWE; -.
DR EvolutionaryTrace; P00324; -.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProt.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001226; Flavodoxin_CS.
DR InterPro; IPR010086; Flavodoxin_lc.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR PIRSF; PIRSF038996; FldA; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR01752; flav_long; 1.
DR PROSITE; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Flavoprotein;
KW FMN; Nitrogen fixation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8694750,
FT ECO:0000269|PubMed:889809"
FT CHAIN 2..180
FT /note="Flavodoxin 2"
FT /id="PRO_0000171605"
FT DOMAIN 4..173
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 10..15
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16131657,
FT ECO:0007744|PDB:1YOB"
FT BINDING 57
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16131657,
FT ECO:0007744|PDB:1YOB"
FT BINDING 61
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16131657,
FT ECO:0007744|PDB:1YOB"
FT BINDING 99
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16131657,
FT ECO:0007744|PDB:1YOB"
FT BINDING 106..108
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16131657,
FT ECO:0007744|PDB:1YOB"
FT BINDING 155
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16131657,
FT ECO:0007744|PDB:1YOB"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:5K9B"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5K9B"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:5K9B"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:5K9B"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:5K9B"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:5K9B"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:5K9B"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5K9B"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:5K9B"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:5K9B"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:5K9B"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5K9B"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:1YOB"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:5K9B"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1YOB"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:5K9B"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5K9B"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5K9B"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:5K9B"
SQ SEQUENCE 180 AA; 19663 MW; 8B1B43F23AB5E8B4 CRC64;
MAKIGLFFGS NTGKTRKVAK SIKKRFDDET MSDALNVNRV SAEDFAQYQF LILGTPTLGE
GELPGLSSDC ENESWEEFLP KIEGLDFSGK TVALFGLGDQ VGYPENYLDA LGELYSFFKD
RGAKIVGSWS TDGYEFESSE AVVDGKFVGL ALDLDNQSGK TDERVAAWLA QIAPEFGLSL
