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Database: UniProt
Entry: A0A0F5AS35_9GAMM
LinkDB: A0A0F5AS35_9GAMM
Original site: A0A0F5AS35_9GAMM 
ID   A0A0F5AS35_9GAMM        Unreviewed;       394 AA.
AC   A0A0F5AS35;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 18.
DE   SubName: Full=Chorismate mutase {ECO:0000313|EMBL:KKA45477.1};
DE            EC=4.2.1.51 {ECO:0000313|EMBL:KKA45477.1};
DE            EC=5.4.99.5 {ECO:0000313|EMBL:KKA45477.1};
GN   Name=pheA {ECO:0000313|EMBL:KKA45477.1};
GN   ORFNames=WN56_05910 {ECO:0000313|EMBL:KKA45477.1};
OS   Salinivibrio sp. KP-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Salinivibrio; unclassified Salinivibrio.
OX   NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA45477.1, ECO:0000313|Proteomes:UP000033449};
RN   [1] {ECO:0000313|EMBL:KKA45477.1, ECO:0000313|Proteomes:UP000033449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KP-1 {ECO:0000313|EMBL:KKA45477.1,
RC   ECO:0000313|Proteomes:UP000033449};
RA   Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA   Kaur N., Bala M., Mayilraj S.;
RT   "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT   nov., a novel halotolerant gammaproteobacterium isolated from marine
RT   sediment and emended description of the genus Salinivibrio.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKA45477.1}.
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DR   EMBL; LAQR01000002; KKA45477.1; -; Genomic_DNA.
DR   RefSeq; WP_046074132.1; NZ_LAQR01000002.1.
DR   EnsemblBacteria; KKA45477; KKA45477; WN56_05910.
DR   PATRIC; fig|1406902.3.peg.1214; -.
DR   Proteomes; UP000033449; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000313|EMBL:KKA45477.1};
KW   Lyase {ECO:0000313|EMBL:KKA45477.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033449}.
FT   DOMAIN          2..93
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          107..287
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          301..378
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   COILED          8..28
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         12
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         29
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         40
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         49
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         53
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         85
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   BINDING         89
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-1"
FT   SITE            280
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   394 AA;  44120 MW;  0F988719D3B476FC CRC64;
     MPDTPRPLDE IRTRISQLDQ ELLTLLAERR RLSLDVAKNK VAVQKPIRDQ AREQALLEKL
     VTKAQDHQLD AHYVLSLFHT IIEDSVLIQQ RYLQNLANPD NQRPVARVSF LGNQGSYSYL
     AARQYFSRKQ TELVEMACDS FKKVVETVET GHADYGILPV ENTSSGSINE VYDQLQHTRL
     SIVGELTLPI DHCLLTVGDQ DPSQIDTLYA HPQPHQQCSE YIDTLGKVKK IYCSSTAEAM
     QQVADLNQPN VAAIGHAASG EFYGLTAIKS EIANQQQNHT RFIVVARKPV KVSSLTPAKT
     TFIMSTSQQA GSLVECLMVL RERGINMTKL ESRPVLGNPW EEMFYVDVEA NMASNLMQSA
     LDELTTLTRY LKVLGCYPSE TISPTEVSLP DSNE
//
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