AROG_BACSU
ID AROG_BACSU Reviewed; 358 AA.
AC P39912;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein AroA(G);
DE Includes:
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase;
DE EC=2.5.1.54;
DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE AltName: Full=DAHP synthase;
DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
DE Includes:
DE RecName: Full=Chorismate mutase;
DE EC=5.4.99.5;
GN Name=aroA; OrderedLocusNames=BSU29750;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7496534; DOI=10.1099/13500872-141-9-2219;
RA Bolotin A.P., Khazak V.E., Stoynova N., Ratmanova K., Yomantas Y.,
RA Kozlov Y.;
RT "Identical amino acid sequence of the aroA(G) gene products of Bacillus
RT subtilis 168 and B. subtilis Marburg strain.";
RL Microbiology 141:2219-2222(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR EMBL; X65945; CAA46760.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00298.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14953.1; -; Genomic_DNA.
DR PIR; S21418; S21418.
DR RefSeq; NP_390853.1; NC_000964.3.
DR RefSeq; WP_003223454.1; NZ_JNCM01000036.1.
DR PDB; 5GMU; X-ray; 1.80 A; A/B=1-90.
DR PDB; 5GO2; X-ray; 1.91 A; A/B/C/D=1-90.
DR PDBsum; 5GMU; -.
DR PDBsum; 5GO2; -.
DR AlphaFoldDB; P39912; -.
DR SMR; P39912; -.
DR STRING; 224308.BSU29750; -.
DR iPTMnet; P39912; -.
DR jPOST; P39912; -.
DR PaxDb; P39912; -.
DR PRIDE; P39912; -.
DR EnsemblBacteria; CAB14953; CAB14953; BSU_29750.
DR GeneID; 64304693; -.
DR GeneID; 937853; -.
DR KEGG; bsu:BSU29750; -.
DR PATRIC; fig|224308.179.peg.3233; -.
DR eggNOG; COG1605; Bacteria.
DR eggNOG; COG2876; Bacteria.
DR InParanoid; P39912; -.
DR OMA; FRGIPTM; -.
DR PhylomeDB; P39912; -.
DR BioCyc; BSUB:BSU29750-MON; -.
DR BioCyc; MetaCyc:AROABACSU-MON; -.
DR BRENDA; 2.5.1.54; 658.
DR BRENDA; 5.4.99.5; 658.
DR UniPathway; UPA00053; UER00084.
DR UniPathway; UPA00120; UER00203.
DR PRO; PR:P39912; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.59.10; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010954; Chorismate_mutase_GmP-bac.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006268; DAHP_syn_2.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR SMART; SM00830; CM_2; 1.
DR TIGRFAMs; TIGR01801; CM_A; 1.
DR TIGRFAMs; TIGR01361; DAHP_synth_Bsub; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Isomerase; Multifunctional enzyme; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..358
FT /note="Protein AroA(G)"
FT /id="PRO_0000140827"
FT DOMAIN 1..90
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT HELIX 5..37
FT /evidence="ECO:0007829|PDB:5GMU"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:5GMU"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5GMU"
FT HELIX 68..87
FT /evidence="ECO:0007829|PDB:5GMU"
SQ SEQUENCE 358 AA; 39539 MW; 95D217477A2DE5AC CRC64;
MSNTELELLR QKADELNLQI LKLINERGNV VKEIGKAKEA QGVNRFDPVR ERTMLNNIIE
NNDGPFENST IQHIFKEIFK AGLELQEEDH SKALLVSRKK KPEDTIVDIK GEKIGDGQQR
FIVGPCAVES YEQVAEVAAA AKKQGIKILR GGAFKPRTSP YDFQGLGVEG LQILKRVADE
FDLAVISEIV TPAHIEEALD YIDVIQIGAR NMQNFELLKA AGAVKKPVLL KRGLAATISE
FINAAEYIMS QGNDQIILCE RGIRTYETAT RNTLDISAVP ILKQETHLPV FVDVTHSTGR
RDLLLPTAKA ALAIGADGVM AEVHPDPSVA LSDSAQQMAI PEFEKWLNEL KPMVKVNA
