ID B1KL53_SHEWM Unreviewed; 452 AA.
AC B1KL53;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 OrderedLocusNames=Swoo_0093 {ECO:0000313|EMBL:ACA84394.1};
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA84394.1, ECO:0000313|Proteomes:UP000002168};
RN [1] {ECO:0000313|EMBL:ACA84394.1, ECO:0000313|Proteomes:UP000002168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., 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 Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) 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}.
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DR EMBL; CP000961; ACA84394.1; -; Genomic_DNA.
DR RefSeq; WP_012322743.1; NC_010506.1.
DR AlphaFoldDB; B1KL53; -.
DR STRING; 392500.Swoo_0093; -.
DR KEGG; swd:Swoo_0093; -.
DR eggNOG; COG1169; Bacteria.
DR HOGENOM; CLU_006493_8_4_6; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00163.
DR Proteomes; UP000002168; Chromosome.
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:UP000002168}.
FT DOMAIN 190..441
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 209
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT ACT_SITE 259
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT BINDING 437
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
SQ SEQUENCE 452 AA; 51270 MW; 5316A209917D2CCD CRC64;
MAVYSLSQAI ASLTDTLKQL KFQTQSDPII QLSVSIKPVP AIAWLAAQPC YPRIYWKGRD
TEEEVAAIGC CKDFFYADNI DDNQLSIEYQ KQRALSNNQD IRYYGGVAFD RTTECWPEFG
RAHFVLPRVE LRRHGNDYKL LVNLNCETGN AESERDQAMT SLAQLASPKP LPPPNKINIL
SRSDRPDRYR WTELVNQVTH QKFIQETPKV VLSRLTQLEI NQPVDPWMLL ACWQGRNKNS
FQFGFQFSPD STFISCTPER LYRRRQRELF TEALAGTTTR GLNLEEDKVL AQTLMEDNKN
SHENRLVKDH IVDALTPLSN YVGAESIPKV FKLSHIQHLH RSIRAELKPG VDDFQLLQAL
HPTPAVGGLP KEPAMSFIRQ SEGYARGWYA GACGYFNKYE SEFAVAIRSA LIEPGRINLF
AGAGIVSGSE ADSEWIELEN KLTTILSILT EL
//
