UniProt: D4MVS1

Database: UniProt
Entry: D4MVS1_ANAHA

LinkDB:  D4MVS1_ANAHA 
Original site:  D4MVS1_ANAHA

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (6)   
   EMBL (6)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (19)   

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ID   D4MVS1_ANAHA            Unreviewed;       342 AA.
AC   D4MVS1;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE            EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN   Name=aroG {ECO:0000313|EMBL:CUM77922.1};
GN   ORFNames=CL2_26650 {ECO:0000313|EMBL:CBL39487.1}, DO83_10225
GN   {ECO:0000313|EMBL:AQP39919.1}, ERS852425_00572
GN   {ECO:0000313|EMBL:CUM77922.1}, ERS852475_01207
GN   {ECO:0000313|EMBL:CUO02429.1}, ERS852520_02194
GN   {ECO:0000313|EMBL:CUP78333.1}, ERS852571_01290
GN   {ECO:0000313|EMBL:CUM90473.1};
OS   Anaerostipes hadrus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL39487.1, ECO:0000313|Proteomes:UP000008960};
RN   [1] {ECO:0000313|EMBL:CBL39487.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL39487.1,
RC   ECO:0000313|Proteomes:UP000008960};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SSC/2.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL39487.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL39487.1,
RC   ECO:0000313|Proteomes:UP000008960};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000095553, ECO:0000313|Proteomes:UP000095564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5608868 {ECO:0000313|EMBL:CUM77922.1,
RC   ECO:0000313|Proteomes:UP000095598}, 2789STDY5834860
RC   {ECO:0000313|EMBL:CUO02429.1, ECO:0000313|Proteomes:UP000095611},
RC   2789STDY5834908 {ECO:0000313|EMBL:CUP78333.1,
RC   ECO:0000313|Proteomes:UP000095564}, and 2789STDY5834959
RC   {ECO:0000313|EMBL:CUM90473.1, ECO:0000313|Proteomes:UP000095553};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AQP39919.1, ECO:0000313|Proteomes:UP000188159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPB5 {ECO:0000313|EMBL:AQP39919.1,
RC   ECO:0000313|Proteomes:UP000188159};
RX   PubMed=27264309; DOI=10.1038/srep27572;
RA   Zhang Q., Wu Y., Wang J., Wu G., Long W., Xue Z., Wang L., Zhang X.,
RA   Pang X., Zhao Y., Zhao L., Zhang C.;
RT   "Accelerated dysbiosis of gut microbiota during aggravation of DSS-induced
RT   colitis by a butyrate-producing bacterium.";
RL   Sci. Rep. 6:27572-27572(2016).
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and
CC       D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC       heptulosonate-7-phosphate (DAHP). {ECO:0000256|ARBA:ARBA00003726,
CC       ECO:0000256|PIRNR:PIRNR001361}.
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:0000256|ARBA:ARBA00001370,
CC         ECO:0000256|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7. {ECO:0000256|ARBA:ARBA00004688, ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007985, ECO:0000256|PIRNR:PIRNR001361}.
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DR   EMBL; CP012098; AQP39919.1; -; Genomic_DNA.
DR   EMBL; FP929061; CBL39487.1; -; Genomic_DNA.
DR   EMBL; CYXT01000002; CUM77922.1; -; Genomic_DNA.
DR   EMBL; CYXY01000006; CUM90473.1; -; Genomic_DNA.
DR   EMBL; CYZM01000003; CUO02429.1; -; Genomic_DNA.
DR   EMBL; CZAU01000021; CUP78333.1; -; Genomic_DNA.
DR   RefSeq; WP_008390619.1; NZ_WQRB01000046.1.
DR   AlphaFoldDB; D4MVS1; -.
DR   STRING; 649756.ERS852387_02244; -.
DR   GeneID; 15232578; -.
DR   KEGG; bprl:CL2_26650; -.
DR   PATRIC; fig|245018.3.peg.2951; -.
DR   OrthoDB; 9807331at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000008960; Chromosome.
DR   Proteomes; UP000095553; Unassembled WGS sequence.
DR   Proteomes; UP000095564; Unassembled WGS sequence.
DR   Proteomes; UP000095598; Unassembled WGS sequence.
DR   Proteomes; UP000095611; Unassembled WGS sequence.
DR   Proteomes; UP000188159; Chromosome.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DAHP_synth_1.
DR   NCBIfam; TIGR00034; aroFGH; 1.
DR   PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR   PANTHER; PTHR21225:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHE-SENSITIVE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          32..333
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   342 AA;  38293 MW;  5A294F20538568AA CRC64;
     MGMHKIAKMP SPEELKEEMP LSEEAKQIKA ARDKEIRDVF TGASDKFLVI IGPCSADNET
     AVMDYLGRLA RVQKDLADKL LIIPRIYTNK PRTTGDGYKG MVHQPDPEKA PDMASGLRSV
     RKLHMEALEE FHMPAADEML YPGNWPYMED LLSYVAVGAR SVENQQHRLT VSGFDIPAGM
     KNPTGGDLTV MMNSITAGQH QHDFIANGYE VKTDGNPLTH AILRGSVNRH GNNIPNYHYE
     DLTRVAYMYE KFQLKNPAVI VDANHSNSGK QWDQQPRIVQ EVLHSRSFLP EIKSLVKGIM
     IESYIEDGNQ SIGNGVYGQS ITDPCLGWDK SAALLYRMAD YI
//

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