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Database: UniProt
Entry: A0A085G950_9GAMM
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ID   A0A085G950_9GAMM        Unreviewed;       459 AA.
AC   A0A085G950;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Isochorismate synthase MenF {ECO:0000256|HAMAP-Rule:MF_01935};
DE            EC=5.4.4.2 {ECO:0000256|HAMAP-Rule:MF_01935};
DE   AltName: Full=Isochorismate mutase {ECO:0000256|HAMAP-Rule:MF_01935};
GN   Name=menF {ECO:0000256|HAMAP-Rule:MF_01935,
GN   ECO:0000313|EMBL:KFC80245.1};
GN   ORFNames=GEAM_2389 {ECO:0000313|EMBL:KFC80245.1};
OS   Ewingella americana ATCC 33852.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Ewingella.
OX   NCBI_TaxID=910964 {ECO:0000313|EMBL:KFC80245.1, ECO:0000313|Proteomes:UP000028640};
RN   [1] {ECO:0000313|EMBL:KFC80245.1, ECO:0000313|Proteomes:UP000028640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33852 {ECO:0000313|EMBL:KFC80245.1,
RC   ECO:0000313|Proteomes:UP000028640};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of chorismate to isochorismate.
CC       {ECO:0000256|HAMAP-Rule:MF_01935}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985,
CC         ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000799, ECO:0000256|HAMAP-
CC         Rule:MF_01935};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01935};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 1/7.
CC       {ECO:0000256|HAMAP-Rule:MF_01935}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01935}.
CC   -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC       {ECO:0000256|ARBA:ARBA00005297, ECO:0000256|HAMAP-Rule:MF_01935}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFC80245.1}.
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DR   EMBL; JMPJ01000057; KFC80245.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085G950; -.
DR   STRING; 910964.GEAM_2389; -.
DR   eggNOG; COG1169; Bacteria.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00163.
DR   Proteomes; UP000028640; Unassembled WGS sequence.
DR   GO; GO:0008909; F:isochorismate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR   HAMAP; MF_01935; MenF; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR015890; Chorismate_C.
DR   InterPro; IPR004561; IsoChor_synthase.
DR   InterPro; IPR034681; MenF.
DR   InterPro; IPR044250; MenF-like.
DR   NCBIfam; TIGR00543; isochor_syn; 1.
DR   PANTHER; PTHR47253; -; 1.
DR   PANTHER; PTHR47253:SF4; ISOCHORISMATE SYNTHASE 2, CHLOROPLASTIC; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   SUPFAM; SSF56322; ADC synthase; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01935};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01935};
KW   Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01935};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01935};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028640}.
FT   DOMAIN          177..428
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   REGION          440..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT   ACT_SITE        248
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT   BINDING         424
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
SQ   SEQUENCE   459 AA;  51101 MW;  6FB57081F8592E67 CRC64;
     MAVKQISAIL DQLDTALLGT FPDAAGLRQF TYRLPEQPHG GMLEWLDAQP CYPKFYWQQR
     DDAEEVVLCG DAANFSDMPT AQRFLQQYSD FPELRVWGLN AFNDGMGGAQ ASHVLFLPRI
     EITRRDGQCN LRCQLYSPVS LREEADKMRA FLRTLVNSRP LPALKSQVVR YQHLPTQPQW
     ARMIDAVLSG IKQHQFDKVV LARKTTLALS QPLNPASFLA ASRAVNHHCY HFMLAFAPQQ
     AFLGSSPERL FLREKRQLFT EALAGTVAAA DDHQQARALG QWLLNDPKNQ RENMLVVDDI
     CQRLQGGARS LDVMPAEILR LRKVQHLRRS IQAVLAKADD ADCLQRLQPT AAVAGLPRQA
     AREFIARHEP FDRQWYAGSA GYLSLTRSEF TVALRSAAVK GSQLELFAGA GIVAGSDAAQ
     EWLEIENKAA GLRTLLDEGA SSAESAEPQY PELPAVRAG
//
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