(data stored in SCRATCH zone)

SWISSPROT: A8FPH0_SHESH

ID   A8FPH0_SHESH            Unreviewed;       414 AA.
AC   A8FPH0;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 52.
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=Ssed_0130 {ECO:0000313|EMBL:ABV34743.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34743.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34743.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34743.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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: Chorismate = isochorismate.
CC       {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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000821; ABV34743.1; -; Genomic_DNA.
DR   ProteinModelPortal; A8FPH0; -.
DR   STRING; 425104.Ssed_0130; -.
DR   EnsemblBacteria; ABV34743; ABV34743; Ssed_0130.
DR   KEGG; sse:Ssed_0130; -.
DR   eggNOG; ENOG4105E4F; Bacteria.
DR   eggNOG; COG1169; LUCA.
DR   HOGENOM; HOG000028186; -.
DR   KO; K02552; -.
DR   OMA; DEVQLKY; -.
DR   OrthoDB; POG091H09QK; -.
DR   BioCyc; SSED425104:GH7Q-133-MONOMER; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00163.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0008909; F:isochorismate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-HAMAP.
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; A8FPH0.
DR   SWISS-2DPAGE; A8FPH0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Isomerase {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      152    403       Chorismate_bind. {ECO:0000259|Pfam:
FT                                PF00425}.
FT   ACT_SITE    171    171       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01935}.
FT   ACT_SITE    221    221       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01935}.
FT   METAL       265    265       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01935}.
FT   METAL       399    399       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01935}.
SQ   SEQUENCE   414 AA;  47398 MW;  E5AA4BD33D8CDB9A CRC64;
     MPAIAWLAAQ PIYPRIYWKG RDTEEEVAAV GSCKDFAYEE AVDDNQLSLE YQKQRALSNN
     QDIRYYGGVA FDRTTECWPE FGRAHFVLPR IELRRSGEEY KLLINLNCES NDTETERTKA
     IEDLAKLVFP SPLSPPNKIN LLSRSDRPDH YHWTELVKKV THEKFIQDTP KVVLSRLTQL
     EVDEEVDPWT LLACWQGRNQ NSFQFGFQFS PERAFISCTP ERLYRRRQRE LFTEALAGTT
     TRGLNQEEDR VLAQQLLEDS KNSHENQLVK EHIVDALTPL SNYVGAEETP RVFKLSHIQH
     LHRSIRAELK PGIDDFQLLQ ALHPTPAVGG LPKEPAMSFI RQREGYARGW YAGACGYFNK
     YESEFAVAIR SALIEPGRIN LFAGAGIVSG SEPEAEWVEL ENKLTTILSI LTEL
//

If you have problems or comments...

PBIL Back to PBIL home page