Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2-methylcitrate synthase

Gene

gltA

Organism
Antarctic bacterium DS2-3R
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (2S,3S)-2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity.2 Publications

Catalytic activityi

Propanoyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.1 Publication
Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.2 Publications

Kineticsi

Kcat is 8 sec(-1) for 2-methylcitrate synthase activity with propionyl-CoA as substrate (at pH 8 and 23 degrees Celsius). Kcat is 21 sec(-1) for citrate synthase activity with acetyl-CoA as substrate (at pH 8 and 23 degrees Celsius).2 Publications

  1. KM=3 µM for oxaloacetate (with propionyl-CoA at pH 8 and 23 degrees Celsius).1 Publication
  2. KM=6.9 µM for oxaloacetate (with acetyl-CoA at pH 8 and 23 degrees Celsius).1 Publication
  3. KM=7 µM for oxaloacetate (with acetyl-CoA at pH 8 and 23 degrees Celsius).1 Publication
  4. KM=16 µM for propionyl-CoA (at pH 8 and 23 degrees Celsius).1 Publication
  5. KM=229 µM for acetyl-CoA (at pH 8 and 23 degrees Celsius).1 Publication
  6. KM=230 µM for acetyl-CoA (at pH 8 and 23 degrees Celsius).1 Publication

Vmax=12 µmol/min/mg enzyme with propionyl-CoA as substrate (at pH 8 and 23 degrees Celsius).1 Publication

Vmax=30 µmol/min/mg enzyme with acetyl-CoA as substrate (at pH 8 and 23 degrees Celsius).2 Publications

Temperature dependencei

Optimum temperature is 31 degrees Celsius. Cold-active. Is rapidly inactivated at 45 degrees Celsius, and shows significant activity at 10 degrees Celsius and below.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871SubstrateBy similarity
Active sitei222 – 22211 Publication
Active sitei270 – 27011 Publication
Binding sitei279 – 2791Substrate1 Publication
Active sitei321 – 32111 Publication
Binding sitei346 – 3461Substrate1 Publication
Binding sitei365 – 3651SubstrateBy similarity

GO - Molecular functioni

  1. 2-methylcitrate synthase activity Source: UniProtKB
  2. citrate synthase activity Source: UniProtKB

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. propionate metabolic process, methylcitrate cycle Source: UniProtKB
  3. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.
UPA00946.

Names & Taxonomyi

Protein namesi
Recommended name:
2-methylcitrate synthase1 Publication (EC:2.3.3.51 Publication)
Short name:
2-MCS1 Publication
Short name:
MCS1 Publication
Alternative name(s):
(2S,3S)-2-methylcitrate synthaseBy similarity
Citrate synthase1 Publication (EC:2.3.3.162 Publications)
Gene namesi
Name:gltA
Synonyms:cisY
OrganismiAntarctic bacterium DS2-3R
Taxonomic identifieri56673 [NCBI]
Taxonomic lineageiBacteria

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 3793782-methylcitrate synthasePRO_0000169925Add
BLAST

Expressioni

Inductioni

By growth on propionate, but not acetate or glucose.1 Publication

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Beta strandi19 – 246Combined sources
Turni25 – 284Combined sources
Beta strandi29 – 324Combined sources
Helixi37 – 437Combined sources
Helixi46 – 5510Combined sources
Helixi61 – 7212Combined sources
Helixi79 – 857Combined sources
Helixi94 – 10714Combined sources
Turni110 – 1134Combined sources
Helixi117 – 14226Combined sources
Helixi156 – 16510Combined sources
Helixi171 – 18414Combined sources
Helixi191 – 20010Combined sources
Turni201 – 2033Combined sources
Helixi206 – 21813Combined sources
Turni220 – 2245Combined sources
Helixi225 – 23511Combined sources
Helixi244 – 26017Combined sources
Helixi280 – 29314Combined sources
Helixi298 – 31417Combined sources
Helixi321 – 33010Combined sources
Helixi335 – 3373Combined sources
Helixi338 – 35922Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A59X-ray2.09A2-379[»]
ProteinModelPortaliO34002.
SMRiO34002. Positions 3-379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34002.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni264 – 2685Coenzyme A binding1 Publication

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O34002-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEPTIHKGL AGVTADVTAI SKVNSDTNSL LYRGYPVQEL AAKCSFEQVA
60 70 80 90 100
YLLWNSELPN DSELKAFVNF ERSHRKLDEN VKGAIDLLST ACHPMDVART
110 120 130 140 150
AVSVLGANHA RAQDSSPEAN LEKAMSLLAT FPSVVAYDQR RRRGEELIEP
160 170 180 190 200
REDLDYSANF LWMTFGEEAA PEVVEAFNVS MILYAEHSFN ASTFTARVIT
210 220 230 240 250
STLADLHSAV TGAIGALKGP LHGGANEAVM HTFEEIGIRK DESLDEAATR
260 270 280 290 300
SKAWMVDALA QKKKVMGFGH RVYKNGDSRV PTMKSALDAM IKHYDRPEML
310 320 330 340 350
GLYNGLEAAM EEAKQIKPNL DYPAGPTYNL MGFDTEMFTP LFIAARITGW
360 370
TAHIMEQVAD NALIRPLSEY NGPEQRQVP
Length:379
Mass (Da):41,832
Last modified:January 1, 1998 - v1
Checksum:i7D8F4614E3D1CC9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85944 Genomic DNA. Translation: AAC45662.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85944 Genomic DNA. Translation: AAC45662.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A59X-ray2.09A2-379[»]
ProteinModelPortaliO34002.
SMRiO34002. Positions 3-379.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.
UPA00946.

Miscellaneous databases

EvolutionaryTraceiO34002.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R."
    Gerike U., Danson M.J., Russell N.J., Hough D.W.
    Eur. J. Biochem. 248:49-57(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: DS2-3R.
  2. "Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships."
    Gerike U., Hough D.W., Russell N.J., Dyall-Smith M.L., Danson M.J.
    Microbiology 144:929-935(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBSTRATE SPECIFICITY.
    Strain: DS2-3R.
  3. "Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium."
    Russell R.J., Gerike U., Danson M.J., Hough D.W., Taylor G.L.
    Structure 6:351-361(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 2-379 IN COMPLEX WITH COENZYME A AND SUBSTRATE, ACTIVE SITE, SUBUNIT.
    Strain: DS2-3R.

Entry informationi

Entry nameiPRPC_ABDS2
AccessioniPrimary (citable) accession number: O34002
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: April 29, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.