(data stored in ACNUC7421 zone)

SWISSPROT: A0KFN9_AERHH

ID   A0KFN9_AERHH            Unreviewed;       448 AA.
AC   A0KFN9;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 74.
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:ABK38715.1};
GN   OrderedLocusNames=AHA_0532 {ECO:0000313|EMBL:ABK38715.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38715.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK38715.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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|HAMAP-Rule:MF_01935};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01935};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step
CC       1/7. {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|HAMAP-Rule:MF_01935}.
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DR   EMBL; CP000462; ABK38715.1; -; Genomic_DNA.
DR   RefSeq; WP_011704505.1; NC_008570.1.
DR   RefSeq; YP_855065.1; NC_008570.1.
DR   STRING; 380703.AHA_0532; -.
DR   EnsemblBacteria; ABK38715; ABK38715; AHA_0532.
DR   GeneID; 4488872; -.
DR   KEGG; aha:AHA_0532; -.
DR   PATRIC; fig|380703.7.peg.525; -.
DR   eggNOG; ENOG4105E4F; Bacteria.
DR   eggNOG; COG1169; LUCA.
DR   HOGENOM; HOG000028186; -.
DR   KO; K02552; -.
DR   OMA; DEVQLKY; -.
DR   BioCyc; AHYD380703:G1G7B-533-MONOMER; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00163.
DR   Proteomes; UP000000756; 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; -; 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   Pfam; PF00425; Chorismate_bind; 1.
DR   SUPFAM; SSF56322; SSF56322; 1.
DR   TIGRFAMs; TIGR00543; isochor_syn; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFN9.
DR   SWISS-2DPAGE; A0KFN9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01935,
KW   ECO:0000313|EMBL:ABK38715.1};
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:UP000000756}.
FT   DOMAIN      179    439       Chorismate_bind. {ECO:0000259|Pfam:
FT                                PF00425}.
FT   ACT_SITE    200    200       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01935}.
FT   ACT_SITE    258    258       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01935}.
FT   METAL       302    302       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01935}.
FT   METAL       435    435       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01935}.
SQ   SEQUENCE   448 AA;  49673 MW;  9ABF5978598AD18F CRC64;
     MLAQTHIKQQ LDALRHGNAS GFVRLRVAIE VGSFLGWLAA QTLYPRIYWH ARGHDRPEYV
     ALGCLRELTE PQAIRQVCEH TSQPHDDSPR YYGGLAFDPT QPGWQGFGPC RFVLPRIELV
     RRGECVTLCL NLWLPEQTGS DAFEVELQAA AAALDALRPE APLPPLTRHS WQREDCPSQP
     QWQTLVEQVT APEFQAHTPK VVLSRQSRLT HDGATLTADP QAVAPWSLLA SWAQHGQDCF
     HFGFQFSPEQ SFIACSPERL YRREQQHLFT EALAGTIRRS GDEATDAALA AELLADSKNR
     LENRLVHADI LSRLAPLTTD ATLTEPRILK LRLLQHLKCD IEAELKPGVC DWQLLEALHP
     TPAVGGAPRE AALAFIRERE PYDRGWYAGA CGMLSRETSE FSVAIRSARI TAQAITLFAG
     AGIVAGSEPA AEWAELDNKI ANVLSLLG
//

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