ID A0A1G0PEG8_9BACT Unreviewed; 680 AA.
AC A0A1G0PEG8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=3-deoxy-D-arabinoheptulosonate-7-phosphate synthase {ECO:0000313|EMBL:OGU34104.1};
GN ORFNames=A2068_09075 {ECO:0000313|EMBL:OGU34104.1};
OS Ignavibacteria bacterium GWB2_35_6b.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798424 {ECO:0000313|EMBL:OGU34104.1, ECO:0000313|Proteomes:UP000178800};
RN [1] {ECO:0000313|EMBL:OGU34104.1, ECO:0000313|Proteomes:UP000178800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGU34104.1}.
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DR EMBL; MGZW01000222; OGU34104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0PEG8; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000178800; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
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; IPR006268; DAHP_syn_2.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR NCBIfam; TIGR01797; CM_P_1; 1.
DR NCBIfam; TIGR01361; DAHP_synth_Bsub; 1.
DR PANTHER; PTHR43018; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR PANTHER; PTHR43018:SF2; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 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;
FT DOMAIN 1..91
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 105..285
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 299..376
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 396..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 76221 MW; 0CC2AE17D266BA10 CRC64;
MDSKDLPEIR KNINEVDSEI IKLLAKRRKL SKEVIRAKEV SDKPIRDQKR EQDLLNRLIA
FGKENGLDAH FVTKVFYEII DDSVRIQQKY VHKILGEKIN KESIKVSIQG IEGSYSYLAA
NKFFAQYDQG LEFISNKAFE DVVKNVEKGE ADYAMLPIEN TTSGGINEVY DLLLHTTLSI
IGEEKLQVKH CLASTADVPL SKIKRVYAHY QAAAQCSKFL SQMPNCSVEF FPDTAMSVQK
IKEENNPEYA AIASEEAANL FEVKILRDDI ANQSGNFTRF LIAARKPVLV DLRIPSKTSL
VMATSHTPGS LVSALMVFQQ HGINMTKLES RPILGNPWEE MFYLDFEGNL YDENVKSLLD
ELGTHTRFMK ILGCYPSQEL MKTKLDDSQF GEDAIEIKTD EENKAEEKPK PKKKASKSYK
LASREYKSED TIIKVKDVKI GGDGFIIMAG PCSVESREQI FSCASEAKEN GVHILRGGCF
KPRTSPYSFQ GLGYEGLDLL LEAGQSYDLP IITEVLSPEQ VSEVSKKSDI LQVGARNMQN
FSLLTEVGKS HRPVMLKRGL MASIDELLNA AEYILAQGNR QVILCERGIR TFETATRNTL
DLSAIPVLKE LTHLPIIVDP SHAVGVRDMV IPLAKASKVV GAHGIMIEFH PEPEKALSDG
PQALYYNQLE SLMKDLRNIK
//
