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FMNB_DESVM
ID   FMNB_DESVM              Reviewed;         122 AA.
AC   Q46604; B8DML0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=FMN-binding protein;
GN   OrderedLocusNames=DvMF_2023;
OS   Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8119891; DOI=10.1016/s0021-9258(17)37499-9;
RA   Kitamura M., Kojima S., Ogasawara K., Nakaya T., Sagara T., Niki K.,
RA   Miura K., Akutsu H., Kumagai I.;
RT   "Novel FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F).
RT   Cloning and expression of its gene in Escherichia coli.";
RL   J. Biol. Chem. 269:5566-5573(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19637 / Miyazaki F;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA   Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   STRUCTURE BY NMR, AND SEQUENCE REVISION TO 101.
RX   PubMed=9406543; DOI=10.1038/nsb1297-975;
RA   Liepinsh E., Kitamura M., Murakami T., Nakaya T., Otting G.;
RT   "Pathway of chymotrypsin evolution suggested by the structure of the FMN-
RT   binding protein from Desulfovibrio vulgaris (Miyazaki F).";
RL   Nat. Struct. Biol. 4:975-979(1997).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
RX   PubMed=10713530; DOI=10.1107/s0907444900000111;
RA   Suto K., Kawagoe K., Shibata N., Morimoto Y., Higuchi Y., Kitamura M.,
RA   Nakaya T., Yasuoka N.;
RT   "How do the X-ray structure and the NMR structure of FMN-binding protein
RT   differ?";
RL   Acta Crystallogr. D 56:368-371(2000).
CC   -!- FUNCTION: Functions as a redox protein with a potential of -325 mV.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- SUBUNIT: Monomer and homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR   EMBL; D21804; BAA25177.1; -; Genomic_DNA.
DR   EMBL; CP001197; ACL08966.1; -; Genomic_DNA.
DR   PIR; C53203; C53203.
DR   RefSeq; WP_012613139.1; NC_011769.1.
DR   PDB; 1AXJ; NMR; -; A=1-122.
DR   PDB; 1FLM; X-ray; 1.30 A; A/B=1-122.
DR   PDB; 1WLI; X-ray; 1.60 A; A/B=1-122.
DR   PDB; 1WLK; X-ray; 1.90 A; A/B/C/D=1-122.
DR   PDB; 2E83; X-ray; 1.52 A; A/B=1-122.
DR   PDB; 3A20; X-ray; 1.60 A; A/B=1-122.
DR   PDB; 3A6Q; X-ray; 1.40 A; A/B=1-122.
DR   PDB; 3A6R; X-ray; 1.20 A; A/B/C/D=1-122.
DR   PDB; 3AMF; X-ray; 1.60 A; A/B=1-122.
DR   PDB; 3AWH; X-ray; 1.60 A; A/B=1-122.
DR   PDB; 3VY2; X-ray; 1.60 A; A/B=1-122.
DR   PDB; 3VY5; X-ray; 1.40 A; A/B=1-122.
DR   PDB; 3VYA; X-ray; 2.40 A; A=1-122.
DR   PDBsum; 1AXJ; -.
DR   PDBsum; 1FLM; -.
DR   PDBsum; 1WLI; -.
DR   PDBsum; 1WLK; -.
DR   PDBsum; 2E83; -.
DR   PDBsum; 3A20; -.
DR   PDBsum; 3A6Q; -.
DR   PDBsum; 3A6R; -.
DR   PDBsum; 3AMF; -.
DR   PDBsum; 3AWH; -.
DR   PDBsum; 3VY2; -.
DR   PDBsum; 3VY5; -.
DR   PDBsum; 3VYA; -.
DR   AlphaFoldDB; Q46604; -.
DR   SMR; Q46604; -.
DR   DrugBank; DB03247; Flavin mononucleotide.
DR   EnsemblBacteria; ACL08966; ACL08966; DvMF_2023.
DR   KEGG; dvm:DvMF_2023; -.
DR   eggNOG; COG3576; Bacteria.
DR   HOGENOM; CLU_163878_0_0_7; -.
DR   OMA; MVNTWNS; -.
DR   OrthoDB; 1650305at2; -.
DR   EvolutionaryTrace; Q46604; -.
DR   PRO; PR:Q46604; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.30.110.10; -; 1.
DR   InterPro; IPR011576; Pyridox_Oxase_put.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   Pfam; PF01243; Putative_PNPOx; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Transport.
FT   CHAIN           1..122
FT                   /note="FMN-binding protein"
FT                   /id="PRO_0000087315"
FT   CONFLICT        101
FT                   /note="I -> Y (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..9
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   STRAND          15..21
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   STRAND          23..32
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   HELIX           33..35
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   STRAND          43..50
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   HELIX           52..60
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   STRAND          63..74
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   STRAND          76..95
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   HELIX           96..99
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   TURN            100..103
FT                   /evidence="ECO:0007829|PDB:3A6R"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:1AXJ"
FT   STRAND          108..120
FT                   /evidence="ECO:0007829|PDB:3A6R"
SQ   SEQUENCE   122 AA;  13137 MW;  48F67A37773A3528 CRC64;
     MLPGTFFEVL KNEGVVAIAT QGEDGPHLVN TWNSYLKVLD GNRIVVPVGG MHKTEANVAR
     DERVLMTLGS RKVAGRNGPG TGFLIRGSAA FRTDGPEFEA IARFKWARAA LVITVVSAEQ
     TL
 
 
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