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2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) ((2S,3S)-2-methylcitrate synthase) (Citrate synthase) (EC 2.3.3.16)

 PRPC_ABDS2              Reviewed;         379 AA.
O34002;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 86.
RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:9579066};
Short=2-MCS {ECO:0000303|PubMed:9579066};
Short=MCS {ECO:0000303|PubMed:9579066};
EC=2.3.3.5 {ECO:0000269|PubMed:9579066};
AltName: Full=(2S,3S)-2-methylcitrate synthase {ECO:0000250|UniProtKB:P31660};
AltName: Full=Citrate synthase {ECO:0000303|PubMed:9310359};
EC=2.3.3.16 {ECO:0000269|PubMed:9310359, ECO:0000269|PubMed:9579066};
Name=gltA; Synonyms=cisY;
Antarctic bacterium DS2-3R.
Bacteria.
NCBI_TaxID=56673;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, FUNCTION,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=DS2-3R;
PubMed=9310359; DOI=10.1111/j.1432-1033.1997.00049.x;
Gerike U., Danson M.J., Russell N.J., Hough D.W.;
"Sequencing and expression of the gene encoding a cold-active citrate
synthase from an Antarctic bacterium, strain DS2-3R.";
Eur. J. Biochem. 248:49-57(1997).
[2]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
INDUCTION, AND SUBSTRATE SPECIFICITY.
STRAIN=DS2-3R;
PubMed=9579066; DOI=10.1099/00221287-144-4-929;
Gerike U., Hough D.W., Russell N.J., Dyall-Smith M.L., Danson M.J.;
"Citrate synthase and 2-methylcitrate synthase: structural, functional
and evolutionary relationships.";
Microbiology 144:929-935(1998).
[3]
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 2-379 IN COMPLEX WITH
COENZYME A AND SUBSTRATE, ACTIVE SITE, AND SUBUNIT.
STRAIN=DS2-3R;
PubMed=9551556; DOI=10.1016/S0969-2126(98)00037-9;
Russell R.J., Gerike U., Danson M.J., Hough D.W., Taylor G.L.;
"Structural adaptations of the cold-active citrate synthase from an
Antarctic bacterium.";
Structure 6:351-361(1998).
-!- FUNCTION: 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. {ECO:0000269|PubMed:9310359,
ECO:0000269|PubMed:9579066}.
-!- CATALYTIC ACTIVITY: Propanoyl-CoA + H(2)O + oxaloacetate =
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.
{ECO:0000269|PubMed:9579066}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate +
CoA. {ECO:0000269|PubMed:9310359, ECO:0000269|PubMed:9579066}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3 uM for oxaloacetate (with propionyl-CoA at pH 8 and 23
degrees Celsius) {ECO:0000269|PubMed:9579066};
KM=6.9 uM for oxaloacetate (with acetyl-CoA at pH 8 and 23
degrees Celsius) {ECO:0000269|PubMed:9310359};
KM=7 uM for oxaloacetate (with acetyl-CoA at pH 8 and 23 degrees
Celsius) {ECO:0000269|PubMed:9579066};
KM=16 uM for propionyl-CoA (at pH 8 and 23 degrees Celsius)
{ECO:0000269|PubMed:9579066};
KM=229 uM for acetyl-CoA (at pH 8 and 23 degrees Celsius)
{ECO:0000269|PubMed:9579066};
KM=230 uM for acetyl-CoA (at pH 8 and 23 degrees Celsius)
{ECO:0000269|PubMed:9310359};
Vmax=12 umol/min/mg enzyme with propionyl-CoA as substrate (at
pH 8 and 23 degrees Celsius) {ECO:0000269|PubMed:9579066};
Vmax=30 umol/min/mg enzyme with acetyl-CoA as substrate (at pH 8
and 23 degrees Celsius) {ECO:0000269|PubMed:9310359,
ECO:0000269|PubMed:9579066};
Note=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).
{ECO:0000269|PubMed:9310359, ECO:0000269|PubMed:9579066};
Temperature dependence:
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.
{ECO:0000269|PubMed:9310359};
-!- PATHWAY: Organic acid metabolism; propanoate degradation.
{ECO:0000305|PubMed:9579066}.
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
isocitrate from oxaloacetate: step 2/2.
{ECO:0000305|PubMed:9579066}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9310359,
ECO:0000269|PubMed:9551556}.
-!- INDUCTION: By growth on propionate, but not acetate or glucose.
{ECO:0000269|PubMed:9579066}.
-!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U85944; AAC45662.1; -; Genomic_DNA.
PDB; 1A59; X-ray; 2.09 A; A=2-379.
PDBsum; 1A59; -.
ProteinModelPortal; O34002; -.
SMR; O34002; -.
DrugBank; DB04272; Citric Acid.
DrugBank; DB01992; Coenzyme A.
UniPathway; UPA00223; UER00718.
UniPathway; UPA00946; -.
EvolutionaryTrace; O34002; -.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:UniProtKB.
GO; GO:0036440; F:citrate synthase activity; IDA:UniProtKB.
GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IDA:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.580.10; -; 2.
InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
InterPro; IPR002020; Citrate_synthase.
InterPro; IPR019810; Citrate_synthase_AS.
InterPro; IPR024176; Citrate_synthase_bac-typ.
InterPro; IPR036969; Citrate_synthase_sf.
PANTHER; PTHR11739; PTHR11739; 1.
Pfam; PF00285; Citrate_synt; 1.
PIRSF; PIRSF001369; Citrate_synth; 1.
PRINTS; PR00143; CITRTSNTHASE.
SUPFAM; SSF48256; SSF48256; 1.
TIGRFAMs; TIGR01800; cit_synth_II; 1.
PROSITE; PS00480; CITRATE_SYNTHASE; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Transferase;
Tricarboxylic acid cycle.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9310359}.
CHAIN 2 379 2-methylcitrate synthase.
/FTId=PRO_0000169925.
REGION 264 268 Coenzyme A binding.
{ECO:0000269|PubMed:9551556}.
ACT_SITE 222 222 {ECO:0000269|PubMed:9551556}.
ACT_SITE 270 270 {ECO:0000269|PubMed:9551556}.
ACT_SITE 321 321 {ECO:0000269|PubMed:9551556}.
BINDING 187 187 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 279 279 Substrate. {ECO:0000269|PubMed:9551556}.
BINDING 346 346 Substrate. {ECO:0000269|PubMed:9551556}.
BINDING 365 365 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
HELIX 8 10 {ECO:0000244|PDB:1A59}.
STRAND 19 24 {ECO:0000244|PDB:1A59}.
TURN 25 28 {ECO:0000244|PDB:1A59}.
STRAND 29 32 {ECO:0000244|PDB:1A59}.
HELIX 37 43 {ECO:0000244|PDB:1A59}.
HELIX 46 55 {ECO:0000244|PDB:1A59}.
HELIX 61 72 {ECO:0000244|PDB:1A59}.
HELIX 79 85 {ECO:0000244|PDB:1A59}.
HELIX 94 107 {ECO:0000244|PDB:1A59}.
TURN 110 113 {ECO:0000244|PDB:1A59}.
HELIX 117 142 {ECO:0000244|PDB:1A59}.
HELIX 156 165 {ECO:0000244|PDB:1A59}.
HELIX 171 184 {ECO:0000244|PDB:1A59}.
HELIX 191 200 {ECO:0000244|PDB:1A59}.
TURN 201 203 {ECO:0000244|PDB:1A59}.
HELIX 206 218 {ECO:0000244|PDB:1A59}.
TURN 220 224 {ECO:0000244|PDB:1A59}.
HELIX 225 235 {ECO:0000244|PDB:1A59}.
HELIX 244 260 {ECO:0000244|PDB:1A59}.
HELIX 280 293 {ECO:0000244|PDB:1A59}.
HELIX 298 314 {ECO:0000244|PDB:1A59}.
HELIX 321 330 {ECO:0000244|PDB:1A59}.
HELIX 335 337 {ECO:0000244|PDB:1A59}.
HELIX 338 359 {ECO:0000244|PDB:1A59}.
SEQUENCE 379 AA; 41832 MW; 7D8F4614E3D1CC9F CRC64;
MTEPTIHKGL AGVTADVTAI SKVNSDTNSL LYRGYPVQEL AAKCSFEQVA YLLWNSELPN
DSELKAFVNF ERSHRKLDEN VKGAIDLLST ACHPMDVART AVSVLGANHA RAQDSSPEAN
LEKAMSLLAT FPSVVAYDQR RRRGEELIEP REDLDYSANF LWMTFGEEAA PEVVEAFNVS
MILYAEHSFN ASTFTARVIT STLADLHSAV TGAIGALKGP LHGGANEAVM HTFEEIGIRK
DESLDEAATR SKAWMVDALA QKKKVMGFGH RVYKNGDSRV PTMKSALDAM IKHYDRPEML
GLYNGLEAAM EEAKQIKPNL DYPAGPTYNL MGFDTEMFTP LFIAARITGW TAHIMEQVAD
NALIRPLSEY NGPEQRQVP


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