ID F4HAZ1_GALAU Unreviewed; 427 AA.
AC F4HAZ1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=UMN179_01418 {ECO:0000313|EMBL:AEC17437.1};
OS Gallibacterium anatis (strain UMN179) (Pasteurella anatis).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Gallibacterium.
OX NCBI_TaxID=1005058 {ECO:0000313|EMBL:AEC17437.1, ECO:0000313|Proteomes:UP000006908};
RN [1] {ECO:0000313|EMBL:AEC17437.1, ECO:0000313|Proteomes:UP000006908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN179 {ECO:0000313|EMBL:AEC17437.1,
RC ECO:0000313|Proteomes:UP000006908};
RX PubMed=21602325; DOI=10.1128/JB.05177-11;
RA Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., Trampel D.W.,
RA Seemann T.;
RT "Complete genome sequence of Gallibacterium anatis strain UMN179, isolated
RT from a laying hen with peritonitis.";
RL J. Bacteriol. 193:3676-3677(2011).
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; CP002667; AEC17437.1; -; Genomic_DNA.
DR RefSeq; WP_013746210.1; NC_015460.1.
DR AlphaFoldDB; F4HAZ1; -.
DR STRING; 1005058.UMN179_01418; -.
DR KEGG; gan:UMN179_01418; -.
DR PATRIC; fig|1005058.3.peg.1408; -.
DR eggNOG; COG1169; Bacteria.
DR HOGENOM; CLU_006493_8_4_6; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00163.
DR Proteomes; UP000006908; 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}.
FT DOMAIN 164..416
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
FT BINDING 412
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01935"
SQ SEQUENCE 427 AA; 49383 MW; 99F8892C879BAB4A CRC64;
MDVLQQLKSL LTTQIAIYQP DCRRFGEIQA SIEASNIDLI AWLKGQTVFP QFYLQQRQQQ
YQIAAVGAVS HISSFTELSE FKQNYPHFTL VGGVQFRGEV KFILPRLYLH YQQQTLTVKL
LFEQQIWQQE KQQLLQILQQ LPHTQPCNEI KAITPILRHQ SSTQSQWRQL IQRALNTIKQ
QQFNKVVLAR EAVFHLDQPL NGYDFLALSR QTNQYCYHFA VVESAHSMFL GASPECLYRR
TDSQFQTEAL AGTAPIGETD EQQRQYQQWL LQDQKNLLEN QFVVDDICQK IQPYCQKIEV
GNVQLRQLRK VQHLCHPIDA SLQPQHQYWE PLFALHPTAA VAGYPRQAAL SFIKSNEPFQ
RGWYAGAIGV ISHAFAEFCV GLRSAKLTHQ QLHLFAGAGI VKESQADEEW QEIERKMSGL
LSLFERK
//
