ID F9Z4L2_ODOSD Unreviewed; 364 AA.
AC F9Z4L2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000313|EMBL:ADY33697.1};
DE EC=2.5.1.54 {ECO:0000313|EMBL:ADY33697.1};
GN OrderedLocusNames=Odosp_2719 {ECO:0000313|EMBL:ADY33697.1};
OS Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / CIP 104287 / JCM
OS 15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC Odoribacter.
OX NCBI_TaxID=709991 {ECO:0000313|EMBL:ADY33697.1, ECO:0000313|Proteomes:UP000006657};
RN [1] {ECO:0000313|EMBL:ADY33697.1, ECO:0000313|Proteomes:UP000006657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6
RC {ECO:0000313|Proteomes:UP000006657};
RX PubMed=21677857; DOI=10.4056/sigs.1714269;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A., Hammon N.,
RA Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA Rohde M., Detter J.C., Woyke T., Bristow J., Markowitz V., Hugenholtz P.,
RA Eisen J.A., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Odoribacter splanchnicus type strain
RT (1651/6).";
RL Stand. Genomic Sci. 4:200-209(2011).
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DR EMBL; CP002544; ADY33697.1; -; Genomic_DNA.
DR RefSeq; WP_013612890.1; NZ_CP086000.1.
DR AlphaFoldDB; F9Z4L2; -.
DR STRING; 709991.Odosp_2719; -.
DR PaxDb; 709991-Odosp_2719; -.
DR GeneID; 69854889; -.
DR KEGG; osp:Odosp_2719; -.
DR eggNOG; COG1605; Bacteria.
DR eggNOG; COG2876; Bacteria.
DR HOGENOM; CLU_062599_1_1_10; -.
DR OrthoDB; 9780456at2; -.
DR BioCyc; OSPL709991:G1GRN-2768-MONOMER; -.
DR Proteomes; UP000006657; Chromosome.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProt.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
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; IPR006218; DAHP1/KDSA.
DR PANTHER; PTHR43018; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR PANTHER; PTHR43018:SF1; PROTEIN AROA(G); 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000006657};
KW Transferase {ECO:0000313|EMBL:ADY33697.1}.
FT DOMAIN 271..362
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT COILED 263..297
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 364 AA; 41125 MW; 5EC1E601686C29B5 CRC64;
MTATKLDLVK VEDWRLFTDT TKPIIIAGPC SAESEQQVFE TAKGLKAAGV EVLRAGIWKP
RTRPNCFEGV GSEGLVWMKR VQRELGMKIS TEVANVKHVY EALKAGVDML WIGARTSANP
FAMQEIADAL KGTDIPVLVK NPVNPDVELW IGALERLNMA GLKKIGVIHR GFSAYVKSKY
RNVPQWQLPI EIKRRFPDML MICDPSHISG KREYIQEVSQ QAMDLGFDGL IIESHICPEI
ALSDAAQQVT PTSLREILGK LIIRDIDSEN IEYKENIDEL RAQIDDIDND ILELLTRRMK
VSDEIGKYKK QNNITILQPG RWDKILEKVF VKGAETGLDN EFLEKVFKAI HQASIDRQTK
VMNE
//
