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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

Manual assertion based on experiment ini

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

This protein is involved in the pathway propanoate degradation, which is part of Organic acid metabolism.1 Publication
View 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 2 of the subpathway that synthesizes isocitrate from oxaloacetate.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. 2-methylcitrate synthase (gltA)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei187SubstrateBy similarity1
Active sitei2221 Publication1
Active sitei2701 Publication1
Binding sitei279Substrate1 Publication1
Active sitei3211 Publication1
Binding sitei346Substrate1 Publication1
Binding sitei365SubstrateBy similarity1

GO - Molecular functioni

  • 2-methylcitrate synthase activity Source: UniProtKB
  • citrate synthase activity Source: UniProtKB

GO - Biological processi

  • propionate metabolic process, methylcitrate cycle Source: UniProtKB
  • 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

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001699252 – 3792-methylcitrate synthaseAdd BLAST378

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 10Combined sources3
Beta strandi19 – 24Combined sources6
Turni25 – 28Combined sources4
Beta strandi29 – 32Combined sources4
Helixi37 – 43Combined sources7
Helixi46 – 55Combined sources10
Helixi61 – 72Combined sources12
Helixi79 – 85Combined sources7
Helixi94 – 107Combined sources14
Turni110 – 113Combined sources4
Helixi117 – 142Combined sources26
Helixi156 – 165Combined sources10
Helixi171 – 184Combined sources14
Helixi191 – 200Combined sources10
Turni201 – 203Combined sources3
Helixi206 – 218Combined sources13
Turni220 – 224Combined sources5
Helixi225 – 235Combined sources11
Helixi244 – 260Combined sources17
Helixi280 – 293Combined sources14
Helixi298 – 314Combined sources17
Helixi321 – 330Combined sources10
Helixi335 – 337Combined sources3
Helixi338 – 359Combined sources22

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO34002.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni264 – 268Coenzyme A binding1 Publication5

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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A59X-ray2.09A2-379[»]
ProteinModelPortaliO34002.
SMRiO34002.
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.
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...

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: November 2, 2016
This is version 83 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

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 one 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.