AROG_MYCS2
ID AROG_MYCS2 Reviewed; 464 AA.
AC A0R033; I7GBP1;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase AroG;
DE EC=2.5.1.54 {ECO:0000250|UniProtKB:O53512};
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;
GN Name=aroG; OrderedLocusNames=MSMEG_4244, MSMEI_4144;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
CC -!- FUNCTION: Catalyzes an aldol-like condensation reaction between
CC phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate
CC 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic
CC phosphate. {ECO:0000250|UniProtKB:O53512}.
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 Evidence={ECO:0000250|UniProtKB:O53512};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14718;
CC Evidence={ECO:0000250|UniProtKB:O53512};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O53512};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:O53512};
CC Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC Evidence={ECO:0000250|UniProtKB:O53512};
CC Note=Binds 1 divalent cation per subunit. The enzyme is active with
CC manganese, cobalt or cadmium ions. {ECO:0000250|UniProtKB:O53512};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7. {ECO:0000250|UniProtKB:O53512}.
CC -!- SUBUNIT: Homodimer (By similarity). Probably interacts with MSMEG_5536.
CC {ECO:0000250|UniProtKB:O53512}.
CC -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK71107.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40601.1; -; Genomic_DNA.
DR RefSeq; WP_003895637.1; NZ_SIJM01000003.1.
DR RefSeq; YP_888521.1; NC_008596.1.
DR AlphaFoldDB; A0R033; -.
DR SMR; A0R033; -.
DR STRING; 246196.MSMEI_4144; -.
DR PRIDE; A0R033; -.
DR EnsemblBacteria; ABK71107; ABK71107; MSMEG_4244.
DR EnsemblBacteria; AFP40601; AFP40601; MSMEI_4144.
DR GeneID; 66735589; -.
DR KEGG; msg:MSMEI_4144; -.
DR KEGG; msm:MSMEG_4244; -.
DR PATRIC; fig|246196.19.peg.4164; -.
DR eggNOG; COG3200; Bacteria.
DR OMA; KVMMQMA; -.
DR OrthoDB; 1371606at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
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; 3.20.20.70; -; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002480; DAHP_synth_2.
DR PANTHER; PTHR21337; PTHR21337; 1.
DR Pfam; PF01474; DAHP_synth_2; 1.
DR TIGRFAMs; TIGR01358; DAHP_synth_II; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cadmium; Cobalt;
KW Manganese; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..464
FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase AroG"
FT /id="PRO_0000414910"
FT BINDING 87
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 126
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 285..286
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 308
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 339
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 371
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 413
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 443
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O53512"
SQ SEQUENCE 464 AA; 50731 MW; 304334998F0164C1 CRC64;
MNWTVDIPID QLPPLPPLSD ELRQRLDSAL AKPAVQQPSW DPDAAKAMRT VLESVPPVTV
PSEIEKLKGL LADVAQGKAF LLQGGDCAET FVDNTEPHIR ANIRTLLQMA VVLTYGASMP
VVKVARIAGQ YAKPRSSDVD ALGLKSYRGD MINGFAPDAA AREHDPSRLV RAYANASAAM
NLMRALTSSG LASLHLVHEW NREFVRTSPA GARYEALAGE IDRGLNFMSA CGVADRNLQT
AEIFASHEAL VLDYERAMLR LSNPAETDGA AKLYDQSAHY LWIGERTRQL DGAHVAFAEV
IANPIGVKLG PTTTPELAVE YVERLDPNNE PGRLTLVTRM GNNKVRDLLP PIIEKVQATG
HQVIWQCDPM HGNTHESSTG YKTRHFDRIV DEVQGFFEVH HALGTHPGGI HVEITGENVT
ECLGGAQDIS DSDLAGRYET ACDPRLNTQQ SLELAFLVAE MLRD
