ID C5BMH8_TERTT Unreviewed; 462 AA.
AC C5BMH8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:ACR13758.1};
GN OrderedLocusNames=TERTU_2729 {ECO:0000313|EMBL:ACR13758.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR13758.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR13758.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
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; CP001614; ACR13758.1; -; Genomic_DNA.
DR RefSeq; WP_015819873.1; NC_012997.1.
DR AlphaFoldDB; C5BMH8; -.
DR STRING; 377629.TERTU_2729; -.
DR KEGG; ttu:TERTU_2729; -.
DR eggNOG; COG1169; Bacteria.
DR HOGENOM; CLU_006493_8_4_6; -.
DR OrthoDB; 9806579at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00163.
DR Proteomes; UP000009080; 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 NCBIfam; TIGR00543; isochor_syn; 1.
DR PANTHER; PTHR42839; ISOCHORISMATE SYNTHASE ENTC; 1.
DR PANTHER; PTHR42839:SF2; ISOCHORISMATE SYNTHASE ENTC; 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:UP000009080}.
FT DOMAIN 198..449
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT ACT_SITE 267
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
SQ SEQUENCE 462 AA; 50544 MW; AAC5409A1095C64A CRC64;
MSVQSTVSTS GTPSGLLEVL AELRERLRGE KYCAQRLLRV SLPVELDNTP LEIAAACRES
ERQIFATRDN KFTLVGFGHS RRLSTNNAEQ TAAILDQAQQ LVAGSDACWL GGCSFAGNTG
VGRWQEFPAA CFVLPLVELR ETNGFCEVAI NMYAESYAQW QTRLEAIDQL VGEISAIPSL
AGSRLPALVA RRDTISLREW RELVMNALEA IRGGGFKKVV LAREVELCLT APADPFAALA
QLDRQHNPGY LFALTSGKDH FFGCSPERLF KQKGHQLVTE ALAGTVRRGL DGDEDAALES
RLIQSRKLVH EHQLVADAIH SALCPLALQL SPVSDVGVVK LRHIQHSYQK VSAILRPDVS
IGQLFSSLHP TPAICGYPSA QAKAFIRDHE HFQRGWYSGV AGVIGAEHAE FSVAIRSGLA
RGDKVWLYSG VGIVRGSNPV GEWRELESKL QVMLDTLLPH AH
//
