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Q8NSH9 (PRPD1_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
2-methylcitrate dehydratase 1

EC=4.2.1.79
Gene names
Name:prpD1
Ordered Locus Names:Cgl0694, cg0796
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the dehydration of 2-methylcitrate to 2-methyl-cis-aconitate By similarity.

Catalytic activity

(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O.

Miscellaneous

The prpD1B1C1 operon seems not to be involved in propionate degradation.

Sequence similarities

Belongs to the PrpD family.

Ontologies

Keywords
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpropionate catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_function2-methylcitrate dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4984982-methylcitrate dehydratase 1
PRO_0000215021

Sequences

Sequence LengthMass (Da)Tools
Q8NSH9 [UniParc].

Last modified September 19, 2002. Version 1.
Checksum: 626F96A36B9227C3

FASTA49855,013
        10         20         30         40         50         60 
MRIHDVYTHL SADNFPKAEH LAWKFSELAT DPVEVTPDVS EMIINRIIDN AAVSAASVLR 

        70         80         90        100        110        120 
RPVTVARQQA QSHPREKGGK VFGISGSYSP EWAAFANGVA VRELDFHDTF LAAEYSHPGD 

       130        140        150        160        170        180 
NIPPLLAVAQ AQRSSGRDLI RGIATAYEVQ VELVRGICLH EHKIDHVAHL GPSAAAGLGT 

       190        200        210        220        230        240 
LLHVDEETIY QAIGQALHTT TATRQSRKGE ISSWKAFAPA FAGKMAIEAM DRAMRGEGSP 

       250        260        270        280        290        300 
APIWEGEDGV IAWLLSGKDH VYHVPLPEHG EPKLGILETY TKEHSAEYQS QAPIDLARRM 

       310        320        330        340        350        360 
KPLVDAAGGT EHIAEIVLRT SHHTHYVIGT GANDPQKMDP QASRETLDHS IMYIFAVALQ 

       370        380        390        400        410        420 
DGVWHHEFSY TRKRSTRPET VELWHKIRTV EDPEWTRRYH SDDPAKKAFG AKAVITMADG 

       430        440        450        460        470        480 
TVIEDELAVA DAHPLGARPF ARENYIEKFR TLAQGIVIDS EQERFLHAVQ SLPDLDDLDQ 

       490 
LNIEVDISNQ AATKAGLL 

« Hide

References

« Hide 'large scale' references
[1]"Identification of two prpDBC gene clusters in Corynebacterium glutamicum and their involvement in propionate degradation via the 2-methylcitrate cycle."
Claes W.A., Puehler A., Kalinowski J.
J. Bacteriol. 184:2728-2739(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF434798 Genomic DNA. Translation: AAM21500.1.
BA000036 Genomic DNA. Translation: BAB98087.1.
BX927150 Genomic DNA. Translation: CAF19399.1.
RefSeqNP_599926.1. NC_003450.3.
YP_224985.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NSH9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg0796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB98087; BAB98087; BAB98087.
CAF19399; CAF19399; cg0796.
GeneID1018693.
KEGGcgb:cg0796.
cgl:NCgl0664.
PATRIC21493430. VBICorGlu203724_0680.

Phylogenomic databases

eggNOGCOG2079.
HOGENOMHOG000242813.
KOK01720.
OMAFRREEGI.
OrthoDBEOG6RC3K5.

Family and domain databases

InterProIPR005656. MmgE_PrpD.
[Graphical view]
PANTHERPTHR16943. PTHR16943. 1 hit.
PfamPF03972. MmgE_PrpD. 1 hit.
[Graphical view]
SUPFAMSSF103378. SSF103378. 1 hit.
ProtoNetSearch...

Entry information

Entry namePRPD1_CORGL
AccessionPrimary (citable) accession number: Q8NSH9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: July 9, 2014
This is version 65 of the entry and version 1 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