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Protein

Protein AroA(G)

Gene

aroA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.
Chorismate = prephenate.

Pathwayi: chorismate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Protein AroA(G) (aroA)
  2. 3-dehydroquinate synthase (aroB), 3-dehydroquinate synthase (aroB)
  3. 3-dehydroquinate dehydratase (aroD), 3-dehydroquinate dehydratase (yqhS)
  4. Shikimate dehydrogenase (NADP(+)) (aroE)
  5. Shikimate kinase (aroK)
  6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
  7. Chorismate synthase (aroF), Chorismate synthase (aroC)
This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

Pathwayi: prephenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes prephenate from chorismate.
Proteins known to be involved in this subpathway in this organism are:
  1. Chorismate mutase AroH (aroH), Chorismate mutase AroH (aroH), Protein AroA(G) (aroA)
This subpathway is part of the pathway prephenate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes prephenate from chorismate, the pathway prephenate biosynthesis and in Metabolic intermediate biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU29750-MONOMER.
UniPathwayiUPA00053; UER00084.
UPA00120; UER00203.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein AroA(G)
Including the following 2 domains:
Phospho-2-dehydro-3-deoxyheptonate aldolase (EC:2.5.1.54)
Alternative name(s):
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
DAHP synthase
Phospho-2-keto-3-deoxyheptonate aldolase
Chorismate mutase (EC:5.4.99.5)
Gene namesi
Name:aroA
Ordered Locus Names:BSU29750
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Protein AroA(G)PRO_0000140827Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP39912.

PTM databases

iPTMnetiP39912.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100016231.

Structurei

3D structure databases

ProteinModelPortaliP39912.
SMRiP39912. Positions 9-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090Chorismate mutasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class-I DAHP synthase family.Curated
Contains 1 chorismate mutase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CXR. Bacteria.
COG1605. LUCA.
COG2876. LUCA.
HOGENOMiHOG000023020.
InParanoidiP39912.
KOiK13853.
OMAiEHNDGPF.
OrthoDBiEOG657JFQ.
PhylomeDBiP39912.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002701. Chorismate_mutase.
IPR010954. Chorismate_mutase_GmP-bac.
IPR020822. Chorismate_mutase_type_II.
IPR006218. DAHP1/KDSA.
IPR006268. DAHP_syn_2.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
PF00793. DAHP_synth_1. 1 hit.
[Graphical view]
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01801. CM_A. 1 hit.
TIGR01361. DAHP_synth_Bsub. 1 hit.
PROSITEiPS51168. CHORISMATE_MUT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39912-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNTELELLR QKADELNLQI LKLINERGNV VKEIGKAKEA QGVNRFDPVR
60 70 80 90 100
ERTMLNNIIE NNDGPFENST IQHIFKEIFK AGLELQEEDH SKALLVSRKK
110 120 130 140 150
KPEDTIVDIK GEKIGDGQQR FIVGPCAVES YEQVAEVAAA AKKQGIKILR
160 170 180 190 200
GGAFKPRTSP YDFQGLGVEG LQILKRVADE FDLAVISEIV TPAHIEEALD
210 220 230 240 250
YIDVIQIGAR NMQNFELLKA AGAVKKPVLL KRGLAATISE FINAAEYIMS
260 270 280 290 300
QGNDQIILCE RGIRTYETAT RNTLDISAVP ILKQETHLPV FVDVTHSTGR
310 320 330 340 350
RDLLLPTAKA ALAIGADGVM AEVHPDPSVA LSDSAQQMAI PEFEKWLNEL

KPMVKVNA
Length:358
Mass (Da):39,539
Last modified:February 1, 1995 - v1
Checksum:i95D217477A2DE5AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65945 Genomic DNA. Translation: CAA46760.1.
AF008220 Genomic DNA. Translation: AAC00298.1.
AL009126 Genomic DNA. Translation: CAB14953.1.
PIRiS21418.
RefSeqiNP_390853.1. NC_000964.3.
WP_003223454.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14953; CAB14953; BSU29750.
GeneIDi11240568.
937853.
KEGGibsu:BSU29750.
PATRICi18977858. VBIBacSub10457_3117.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65945 Genomic DNA. Translation: CAA46760.1.
AF008220 Genomic DNA. Translation: AAC00298.1.
AL009126 Genomic DNA. Translation: CAB14953.1.
PIRiS21418.
RefSeqiNP_390853.1. NC_000964.3.
WP_003223454.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP39912.
SMRiP39912. Positions 9-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100016231.

PTM databases

iPTMnetiP39912.

Proteomic databases

PaxDbiP39912.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14953; CAB14953; BSU29750.
GeneIDi11240568.
937853.
KEGGibsu:BSU29750.
PATRICi18977858. VBIBacSub10457_3117.

Phylogenomic databases

eggNOGiENOG4105CXR. Bacteria.
COG1605. LUCA.
COG2876. LUCA.
HOGENOMiHOG000023020.
InParanoidiP39912.
KOiK13853.
OMAiEHNDGPF.
OrthoDBiEOG657JFQ.
PhylomeDBiP39912.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00084.
UPA00120; UER00203.
BioCyciBSUB:BSU29750-MONOMER.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002701. Chorismate_mutase.
IPR010954. Chorismate_mutase_GmP-bac.
IPR020822. Chorismate_mutase_type_II.
IPR006218. DAHP1/KDSA.
IPR006268. DAHP_syn_2.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
PF00793. DAHP_synth_1. 1 hit.
[Graphical view]
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01801. CM_A. 1 hit.
TIGR01361. DAHP_synth_Bsub. 1 hit.
PROSITEiPS51168. CHORISMATE_MUT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identical amino acid sequence of the aroA(G) gene products of Bacillus subtilis 168 and B. subtilis Marburg strain."
    Bolotin A.P., Khazak V.E., Stoynova N., Ratmanova K., Yomantas Y., Kozlov Y.
    Microbiology 141:2219-2222(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
    Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
    Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
    Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
    Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: 168.

Entry informationi

Entry nameiAROG_BACSU
AccessioniPrimary (citable) accession number: P39912
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 17, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.