ID A0A411PK50_9GAMM Unreviewed; 643 AA.
AC A0A411PK50;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Chorismate mutase {ECO:0000313|EMBL:QBF83935.1};
DE EC=5.4.99.5 {ECO:0000313|EMBL:QBF83935.1};
GN ORFNames=EXU30_15535 {ECO:0000313|EMBL:QBF83935.1};
OS Shewanella maritima.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=2520507 {ECO:0000313|EMBL:QBF83935.1, ECO:0000313|Proteomes:UP000291106};
RN [1] {ECO:0000313|EMBL:QBF83935.1, ECO:0000313|Proteomes:UP000291106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D4-2 {ECO:0000313|EMBL:QBF83935.1,
RC ECO:0000313|Proteomes:UP000291106};
RA Baek K.;
RT "Shewanella sp. D4-2 isolated from Dokdo Island.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00000913};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004741}.
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DR EMBL; CP036200; QBF83935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411PK50; -.
DR KEGG; smai:EXU30_15535; -.
DR OrthoDB; 9802281at2; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000291106; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:UniProtKB-UniPathway.
DR CDD; cd04905; ACT_CM-PDT; 1.
DR CDD; cd13631; PBP2_Ct-PDT_like; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR010952; CM_P_1.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR NCBIfam; TIGR01797; CM_P_1; 1.
DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR Pfam; PF00800; PDT; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Isomerase {ECO:0000313|EMBL:QBF83935.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}.
FT DOMAIN 1..92
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 106..286
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 300..377
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 643 AA; 70520 MW; 15C23BCD865668C7 CRC64;
MQKPPALNDT REQITHLDKE LLGLLAKRRA LSLDVARSKE VDVRPIRDTQ REKELLERLV
HQGREQGLDA HYVISLYQSI IEDSVLNQQA YLHTKANPET QKTRYTVAYL GARGSYSYLA
ANRYCERRQV EMQDLGCPNF DDIITAVESG HADYGFLPIE NTSSGSINEV YDVLQHTSLS
IVGETTIEVG HCMLASSGSS VDNITTLYAH PQPISQCSRY LSQYPHIKLE YCSSSAEAMQ
KVIDSGSLNV AAIGSAEGGA LYGLSAIDKD LANQKINQSR FIVVARKAVD VPSQLPAKTT
LIMATGHKPG ALVEALLVLK EHNLNMSKLE SRPIPGTPWE EMFYLDIDGN LATDNVQQAI
NELERQTRFI KVLGCYPCET VKPTQLSQSQ LLIEPDSSKV ASNQLGHNPK HAKSFKDKDT
VVQLGMMQIG GAALNTIKHL DYTDNNTEVA TQAREAKEAG FEAIVLNNAD LISNEQQVSD
CVKQINLAGL ACILPVEHSV ELPVAAKLSD GLLLQGKSMF DAELLNAAGA LSTPVLIDRH
NNASLEQWLN SADVILNQGN QQIGLVDSGI RGLNEAQKLS LDLSSLIEVK QLTHLPVLVN
LTQTATVETV EQQARAIKQL GLNGVMLDRQ QDQPQLLQRV LAS
//
