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Q9S3U4 (TRPF_ZYMMT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-(5'-phosphoribosyl)anthranilate isomerase

Short name=PRAI
EC=5.3.1.24
Gene names
Name:trpF
Ordered Locus Names:Zymop_0633
OrganismZymomonas mobilis subsp. pomaceae (strain ATCC 29192 / JCM 10191 / NBRC 13757 / NCIMB 11200 / NRRL B-4491) [Complete proteome] [HAMAP]
Taxonomic identifier579138 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00135

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_00135

Sequence similarities

Belongs to the TrpF family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
Tryptophan biosynthesis
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtryptophan biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionphosphoribosylanthranilate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135
PRO_0000154396

Experimental info

Sequence conflict101I → L in AAD51337. Ref.1
Sequence conflict13 – 2614PETLL…NGASH → EETVETAVRYGADY in AAD51337. Ref.1
Sequence conflict38 – 458AVQPEMAS → SVTPEKAA in AAD51337. Ref.1
Sequence conflict49 – 502NR → RQ in AAD51337. Ref.1
Sequence conflict55 – 562ID → VQ in AAD51337. Ref.1
Sequence conflict611L → F in AAD51337. Ref.1
Sequence conflict661D → N in AAD51337. Ref.1
Sequence conflict72 – 754VVHA → ALAS in AAD51337. Ref.1
Sequence conflict881P → A in AAD51337. Ref.1
Sequence conflict91 – 966VAFIRR → IASIRE in AAD51337. Ref.1
Sequence conflict108 – 1114PITR → SIAN in AAD51337. Ref.1
Sequence conflict116 – 1194DQTL → AQAP in AAD51337. Ref.1
Sequence conflict1251V → A in AAD51337. Ref.1
Sequence conflict1281V → L in AAD51337. Ref.1
Sequence conflict1371A → V in AAD51337. Ref.1
Sequence conflict1441K → R in AAD51337. Ref.1
Sequence conflict153 – 1597DYNHPMA → EYKHPLP in AAD51337. Ref.1
Sequence conflict1691D → H in AAD51337. Ref.1
Sequence conflict1851V → I in AAD51337. Ref.1
Sequence conflict1921A → S in AAD51337. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9S3U4 [UniParc].

Last modified December 14, 2011. Version 2.
Checksum: 385307A59D1F856E

FASTA21123,262
        10         20         30         40         50         60 
MSVRTKICGI STPETLLAAV KNGASHIGFV FFEKSPRAVQ PEMASMLINR IPDHIDKIGV 

        70         80         90        100        110        120 
LVDPDDNLLE RVVHAGLTGF QLHGHETPER VAFIRRTFPK VKIWKALPIT RSQDLDQTLH 

       130        140        150        160        170        180 
YRGLVDRVLY DARTDGALPG GMGKRFDWRL LKDYNHPMAW ALSGGLDADN IAQAVAITGA 

       190        200        210 
ELVDVSSGVE TAPGIKDMDK IAQFLQAVRL L 

« Hide

References

« Hide 'large scale' references
[1]"Zymomonas trpFBA genes."
Eddy C.K., Ingram L.O.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29192 / JCM 10191 / NBRC 13757 / NCIMB 11200 / NRRL B-4491.
[2]"Genome sequence of the ethanol-producing Zymomonas mobilis subsp. pomaceae lectotype strain ATCC 29192."
Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., Han C.S., Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., Pappas K.M.
J. Bacteriol. 193:5049-5050(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29192 / JCM 10191 / NBRC 13757 / NCIMB 11200 / NRRL B-4491.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF173835 Genomic DNA. Translation: AAD51337.1.
CP002865 Genomic DNA. Translation: AEI37535.1.
RefSeqYP_004661825.1. NC_015709.1.

3D structure databases

ProteinModelPortalQ9S3U4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEI37535; AEI37535; Zymop_0633.
GeneID10882561.
KEGGzmp:Zymop_0633.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01817.

Enzyme and pathway databases

BioCycZMOB579138:GJDN-656-MONOMER.
UniPathwayUPA00035; UER00042.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00135. PRAI.
InterProIPR013785. Aldolase_TIM.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRPF_ZYMMT
AccessionPrimary (citable) accession number: Q9S3U4
Secondary accession number(s): F8ERS7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: December 14, 2011
Last modified: February 19, 2014
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways