ID A0A0E3U3W8_9ENTR Unreviewed; 376 AA.
AC A0A0E3U3W8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=chorismate mutase {ECO:0000256|ARBA:ARBA00012404};
DE EC=5.4.99.5 {ECO:0000256|ARBA:ARBA00012404};
GN Name=tyrA {ECO:0000313|EMBL:AKC60352.1};
GN ORFNames=BOBLI757_179 {ECO:0000313|EMBL:AKC60352.1};
OS Blochmannia endosymbiont of Camponotus (Colobopsis) obliquus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=1505597 {ECO:0000313|EMBL:AKC60352.1, ECO:0000313|Proteomes:UP000033104};
RN [1] {ECO:0000313|EMBL:AKC60352.1, ECO:0000313|Proteomes:UP000033104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=757 {ECO:0000313|EMBL:AKC60352.1,
RC ECO:0000313|Proteomes:UP000033104};
RX PubMed=25861561;
RA Williams L.E., Wernegreen J.J.;
RT "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene loss
RT among Blochmannia spanning the origin of the ant tribe Camponotini.";
RL PeerJ 3:E881-E881(2015).
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DR EMBL; CP010049; AKC60352.1; -; Genomic_DNA.
DR RefSeq; WP_046304696.1; NZ_CP010049.1.
DR AlphaFoldDB; A0A0E3U3W8; -.
DR STRING; 1505597.BOBLI757_179; -.
DR KEGG; ben:BOBLI757_179; -.
DR PATRIC; fig|1505597.4.peg.174; -.
DR HOGENOM; CLU_036672_1_1_6; -.
DR OrthoDB; 6198144at2; -.
DR UniPathway; UPA00120; UER00203.
DR Proteomes; UP000033104; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR011277; CM_T.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR046825; PDH_C.
DR InterPro; IPR003099; Prephen_DH.
DR NCBIfam; TIGR01799; CM_T; 1.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF20463; PDH_C; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000033104}.
FT DOMAIN 1..90
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 100..364
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 376 AA; 44261 MW; 30100055122B0083 CRC64;
MIQELDVLRN KIDELDKSLL DLLAQRLLLV TQIGELKSRY GLLIHAPDRE EVMLSSRRKE
AIELGISPDL IEDILRRIIR ESYFSENEKG FRNLCPHASR PVVIISNNNN KISKLFNRMF
ILSGYQVKFL EGNDWYIEKE VLKYASIVLI NLSMRLTVEI VKELTYLSDD CILINVFLVK
DISLLKIMLD IHDGPVIGLQ PMFNADIKNM VKQVIVYHEG RMFTKHSWLL DQIKAWGVQL
YHYDSAEHDK NISLSQEFLY FVIFVFGAYL KESNVDLKKI LLLSSSMFRF QMIMIGRFFA
QDPIDYIDII VNSKSCLSLA KSYYQQCIKI LTVLEQGKKQ EFIDYFYHIR HWFSNYAASF
FKESRMLLRY IDDNRK
//
