UniProtKB - Q56063 (PRPC_SALTY)
Protein
2-methylcitrate synthase
Gene
prpC
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Functioni
Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA or butyryl-CoA but with a lower specificity.2 Publications
Catalytic activityi
Kineticsi
Kcat is 1.4 sec(-1) for citrate synthase activity with acetyl-CoA as substrate. Kcat is 1.87 sec(-1) for citrate synthase activity with acetyl-CoA as substrate (at pH 8 and 30 degrees Celsius). Kcat is 7.4 sec(-1) for 2-methylcitrate synthase activity with propionyl-CoA as substrate. Kcat is 8.25 sec(-1) for 2-methylcitrate synthase activity with propionyl-CoA as substrate (at pH 8 and 30 degrees Celsius).2 Publications
- KM=12 µM for oxaloacetate (with propionyl-CoA)1 Publication
- KM=13 µM for oxaloacetate (with propionyl-CoA at pH 8 and 30 degrees Celsius)1 Publication
- KM=14 µM for oxaloacetate (with acetyl-CoA)1 Publication
- KM=15 µM for oxaloacetate (with acetyl-CoA at pH 8 and 30 degrees Celsius)1 Publication
- KM=45 µM for propionyl-CoA (at pH 8 and 30 degrees Celsius)1 Publication
- KM=48 µM for propionyl-CoA1 Publication
- KM=265 µM for acetyl-CoA (at pH 8 and 30 degrees Celsius)1 Publication
- KM=285 µM for acetyl-CoA1 Publication
- Vmax=2 µmol/min/mg enzyme with acetyl-CoA as substrate1 Publication
- Vmax=2.5 µmol/min/mg enzyme with acetyl-CoA as substrate (at pH 8 and 30 degrees Celsius)1 Publication
- Vmax=10 µmol/min/mg enzyme with propionyl-CoA as substrate1 Publication
- Vmax=11 µmol/min/mg enzyme with propionyl-CoA as substrate (at pH 8 and 30 degrees Celsius)1 Publication
: propanoate degradation Pathwayi
This protein is involved in the pathway propanoate degradation, which is part of Organic acid metabolism.1 PublicationView all proteins of this organism that are known to be involved in the pathway propanoate degradation and in Organic acid metabolism.
Pathwayi: tricarboxylic acid cycle
This protein is involved in step 1 of the subpathway that synthesizes isocitrate from oxaloacetate.1 PublicationProteins known to be involved in the 2 steps of the subpathway in this organism are:
- Citrate synthase (gltA), 2-methylcitrate synthase (prpC)
- 2-methylcitrate dehydratase (prpD), Aconitate hydratase A (acnA), Aconitate hydratase B (acnB)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 82 | SubstrateBy similarity | 1 | |
Binding sitei | 200 | SubstrateBy similarity | 1 | |
Active sitei | 235 | By similarity1 Publication | 1 | |
Active sitei | 274 | By similarity1 Publication | 1 | |
Binding sitei | 283 | SubstrateBy similarity | 1 | |
Active sitei | 325 | By similarity1 Publication | 1 | |
Binding sitei | 350 | SubstrateBy similarity | 1 | |
Binding sitei | 369 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- 2-methylcitrate synthase activity Source: UniProtKB
- citrate (Si)-synthase activity Source: GO_Central
- citrate synthase activity Source: UniProtKB
GO - Biological processi
- carbohydrate metabolic process Source: GO_Central
- propionate metabolic process, methylcitrate cycle Source: UniProtKB
- tricarboxylic acid cycle Source: GO_Central
Keywordsi
Molecular function | Transferase |
Biological process | Tricarboxylic acid cycle |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-63 |
BRENDAi | 2.3.3.5, 5542 |
UniPathwayi | UPA00223;UER00717 UPA00946 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:prpC1 Publication Ordered Locus Names:STM0369 |
Organismi | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
Taxonomic identifieri | 99287 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Salmonella › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Cells lacking this gene are unable to accumulate propionyl-CoA.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000169982 | 1 – 389 | 2-methylcitrate synthaseAdd BLAST | 389 |
Proteomic databases
PaxDbi | Q56063 |
PRIDEi | Q56063 |
Interactioni
Subunit structurei
Homodimer at low concentrations and converted to a larger oligomers at higher concentrations.
2 PublicationsStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q56063 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q56063 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 268 – 272 | Coenzyme A bindingBy similarity | 5 |
Sequence similaritiesi
Belongs to the citrate synthase family.Curated
Phylogenomic databases
HOGENOMi | CLU_025068_2_1_6 |
OMAi | NEAVMHM |
PhylomeDBi | Q56063 |
Family and domain databases
Gene3Di | 1.10.230.10, 1 hit 1.10.580.10, 1 hit |
InterProi | View protein in InterPro IPR011278, 2-MeCitrate/Citrate_synth_II IPR016142, Citrate_synth-like_lrg_a-sub IPR016143, Citrate_synth-like_sm_a-sub IPR002020, Citrate_synthase IPR019810, Citrate_synthase_AS IPR024176, Citrate_synthase_bac-typ IPR036969, Citrate_synthase_sf |
PANTHERi | PTHR11739, PTHR11739, 1 hit |
Pfami | View protein in Pfam PF00285, Citrate_synt, 1 hit |
PIRSFi | PIRSF001369, Citrate_synth, 1 hit |
PRINTSi | PR00143, CITRTSNTHASE |
SUPFAMi | SSF48256, SSF48256, 1 hit |
TIGRFAMsi | TIGR01800, cit_synth_II, 1 hit |
PROSITEi | View protein in PROSITE PS00480, CITRATE_SYNTHASE, 1 hit |
i Sequence
Sequence statusi: Complete.
Q56063-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTDTTILQNN THVIKPKKSV ALSGVPAGNT ALCTVGKSGN DLHYRGYDIL
60 70 80 90 100
DLAEHCEFEE VAHLLIHGKL PTRDELNAYK SKLKALRGLP ANVRTVLEAL
110 120 130 140 150
PAASHPMDVM RTGVSALGCT LPEKEGHTVS GARDIADKLL ASLSSILLYW
160 170 180 190 200
YHYSHNGERI QPETDDDSIG GHFLHLLHGE KPTQSWEKAM HISLVLYAEH
210 220 230 240 250
EFNASTFTSR VIAGTGSDVY SAIIGAIGAL RGPKHGGANE VSLEIQQRYE
260 270 280 290 300
TPDEAEADIR KRVENKEVVI GFGHPVYTIA DPRHQVIKRV AKQLSEEGGS
310 320 330 340 350
LKMYHIADRL ETVMWETKKM FPNLDWFSAV SYNMMGVPTE MFTPLFVIAR
360 370 380
VTGWAAHIIE QRQDNKIIRP SANYTGPEDR PFVSIDDRC
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 144 | S → N in AAC44815 (PubMed:9006051).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U51879 Genomic DNA Translation: AAC44815.1 AE006468 Genomic DNA Translation: AAL19323.1 |
RefSeqi | NP_459364.1, NC_003197.2 WP_000132749.1, NC_003197.2 |
Genome annotation databases
EnsemblBacteriai | AAL19323; AAL19323; STM0369 |
GeneIDi | 1251888 |
KEGGi | stm:STM0369 |
PATRICi | fig|99287.12.peg.391 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U51879 Genomic DNA Translation: AAC44815.1 AE006468 Genomic DNA Translation: AAL19323.1 |
RefSeqi | NP_459364.1, NC_003197.2 WP_000132749.1, NC_003197.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3O8J | X-ray | 2.41 | A/B/C/D/E/F/G/H/I/J | 1-389 | [»] | |
SMRi | Q56063 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Proteomic databases
PaxDbi | Q56063 |
PRIDEi | Q56063 |
Genome annotation databases
EnsemblBacteriai | AAL19323; AAL19323; STM0369 |
GeneIDi | 1251888 |
KEGGi | stm:STM0369 |
PATRICi | fig|99287.12.peg.391 |
Phylogenomic databases
HOGENOMi | CLU_025068_2_1_6 |
OMAi | NEAVMHM |
PhylomeDBi | Q56063 |
Enzyme and pathway databases
UniPathwayi | UPA00223;UER00717 UPA00946 |
BioCyci | MetaCyc:MONOMER-63 |
BRENDAi | 2.3.3.5, 5542 |
Miscellaneous databases
EvolutionaryTracei | Q56063 |
Family and domain databases
Gene3Di | 1.10.230.10, 1 hit 1.10.580.10, 1 hit |
InterProi | View protein in InterPro IPR011278, 2-MeCitrate/Citrate_synth_II IPR016142, Citrate_synth-like_lrg_a-sub IPR016143, Citrate_synth-like_sm_a-sub IPR002020, Citrate_synthase IPR019810, Citrate_synthase_AS IPR024176, Citrate_synthase_bac-typ IPR036969, Citrate_synthase_sf |
PANTHERi | PTHR11739, PTHR11739, 1 hit |
Pfami | View protein in Pfam PF00285, Citrate_synt, 1 hit |
PIRSFi | PIRSF001369, Citrate_synth, 1 hit |
PRINTSi | PR00143, CITRTSNTHASE |
SUPFAMi | SSF48256, SSF48256, 1 hit |
TIGRFAMsi | TIGR01800, cit_synth_II, 1 hit |
PROSITEi | View protein in PROSITE PS00480, CITRATE_SYNTHASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PRPC_SALTY | |
Accessioni | Q56063Primary (citable) accession number: Q56063 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | January 23, 2002 | |
Last modified: | December 2, 2020 | |
This is version 124 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families