Reviewed, UniProtKB/Swiss-Prot P74840 (PRPD_SALTY)

Names and origin

Protein names

Recommended name:
    2-methylcitrate dehydratase
    EC=4.2.1.79

Gene names

Name:	prpD
Ordered Locus Names:	STM0370

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the dehydration of 2-methylcitrate to 2-methyl-cis-aconitate. Ref.3
Catalytic activity	(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O.
Cofactor	Binds 1 2Fe-2S cluster By similarity.
Pathway	Organic acid metabolism; propanoate degradation. Ref.3
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the prpD family.

Ontologies

Keywords
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	propionate catabolic process, 2-methylcitrate cycle Inferred from electronic annotation. Source: InterPro
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 2-methylcitrate dehydratase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 483	483	2-methylcitrate dehydratase		PRO_0000215026
Experimental info
	Sequence conflict	308	1	Q → H in AAC44816. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P74840-1 [UniParc]. Last modified January 23, 2002. Version 2. Checksum: CF045F6958157467	FASTA	483	53,787
	10 20 30 40 50 60 MSTQELNIRP DFDREIVDIV DYVMNYEITS KVAYDTAHYC LLDTLGCGLE ALEYPACKKL 70 80 90 100 110 120 LGPIVPGTVV PNGARVPGTQ FQLDPVQAAF NIGAMIRWLD FNDTWLAAEW GHPSDNLGGI 130 140 150 160 170 180 LATADWLSRN AVAAGKAPLT MKQVLSGMIK AHEIQGCIAL ENAFNRVGLD HVLLVKVAST 190 200 210 220 230 240 AVVAEMLGLT RDEILNAVSL AWVDGQSLRT YRHAPNTGTR KSWAAGDATS RAVRLALMAK 250 260 270 280 290 300 TGEMGYPSAL TAKTWGFYDV SFKGETFRFQ RPYGSYVMEN VLFKISFPAE FHSQTAVEAA 310 320 330 340 350 360 MTLYEQMQAA GKTAADIEKV TIRTHEACLR IIDKKGPLNN PADRDHCIQY MVAVPLLFGR 370 380 390 400 410 420 LTAADYEDEV AQDKRIDALR EKIVCYEDPA FTADYHDPEK RAIGNAITVE FTDGSRFGEV 430 440 450 460 470 480 VVEYPIGHAR RRADGIPKLI EKFKINLARQ FPTRQQQRIL DVSLDRARLE QMPVNEYLDL YVI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Propionate catabolism in Salmonella typhimurium LT2: two divergently transcribed units comprise the prp locus at 8.5 centisomes, prpR encodes a member of the sigma-54 family of activators, and the prpBCDE genes constitute an operon." Horswill A.R., Escalante-Semerena J.C. J. Bacteriol. 179:928-940(1997) [PubMed: 9006051] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase enzymes catalyze the conversion of 2-methylcitrate to 2-methylisocitrate." Horswill A.R., Escalante-Semerena J.C. Biochemistry 40:4703-4713(2001) [PubMed: 11294638] [Abstract] Cited for: FUNCTION, PATHWAY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U51879 Genomic DNA. Translation: AAC44816.1. AE006468 Genomic DNA. Translation: AAL19324.1.
RefSeq	NP_459365.1.
3D structure databases
SMR	P74840. Positions 11-483.
ModBase	Search...
Proteomic databases
PRIDE	P74840.
Genome annotation databases
GeneID	1251889.
GenomeReviews	Gene locus STM0370 in contig AE006468_GR.
KEGG	stm:STM0370.
NMPDR	fig|99287.1.peg.356.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P74840.
OMA	ALRFPEC.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-64. STYP99287:STM0370-MON.
BRENDA	4.2.1.79. 2.
Family and domain databases
InterPro	IPR012705. 2Me_IsoCit_deHydtase_PrpD. IPR005656. MmgE_PrpD. [Graphical view]
PANTHER	PTHR16943. MmgE_PrpD. 1 hit.
Pfam	PF03972. MmgE_PrpD. 1 hit. [Graphical view]
TIGRFAMs	TIGR02330. prpD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PRPD_SALTY

Accession

Primary (citable) accession number: P74840

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2002
Last modified:	November 3, 2009
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)