Q8NSH9 (PRPD1_CORGL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-methylcitrate dehydratase 1
EC=4.2.1.79

Gene names

Name:	prpD1
Ordered Locus Names:	Cgl0694, cg0796

Organism

Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]

Taxonomic identifier

196627 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium glutamicum

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Protein existence	Inferred 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 function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	propionate catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	2-methylcitrate dehydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 498	498	2-methylcitrate dehydratase 1		PRO_0000215021

Sequences

	Sequence		Length	Mass (Da)
	Q8NSH9 [UniParc]. Last modified September 19, 2002. Version 1. Checksum: 626F96A36B9227C3	FASTA	498	55,013
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
RefSeq	NP_599926.1. NC_003450.3. YP_224985.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NSH9.
ModBase	Search...
Protein-protein interaction databases
STRING	196627.cg0796.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB98087; BAB98087; BAB98087. CAF19399; CAF19399; cg0796.
GeneID	1018693. 3343519.
KEGG	cgb:cg0796. cgl:NCgl0664.
PATRIC	21493430. VBICorGlu203724_0680.
Phylogenomic databases
eggNOG	COG2079.
HOGENOM	HOG000242813.
KO	K01720.
OMA	IVIDSEQ.
ProtClustDB	CLSK871899.
Enzyme and pathway databases
BioCyc	CGLU196627:GJDM-687-MONOMER.
Family and domain databases
InterPro	IPR005656. MmgE_PrpD. [Graphical view]
PANTHER	PTHR16943. PTHR16943. 1 hit.
Pfam	PF03972. MmgE_PrpD. 1 hit. [Graphical view]
SUPFAM	SSF103378. MmgE_PrpD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PRPD1_CORGL

Accession

Primary (citable) accession number: Q8NSH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	September 19, 2002
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program