PRPC_ABDS2
ID PRPC_ABDS2 Reviewed; 379 AA.
AC O34002;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:9579066};
DE Short=2-MCS {ECO:0000303|PubMed:9579066};
DE Short=MCS {ECO:0000303|PubMed:9579066};
DE EC=2.3.3.5 {ECO:0000269|PubMed:9579066};
DE AltName: Full=Citrate synthase {ECO:0000303|PubMed:9310359};
DE EC=2.3.3.16 {ECO:0000269|PubMed:9310359, ECO:0000269|PubMed:9579066};
GN Name=gltA; Synonyms=cisY;
OS Antarctic bacterium DS2-3R.
OC Bacteria.
OX NCBI_TaxID=56673;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=DS2-3R;
RX PubMed=9310359; DOI=10.1111/j.1432-1033.1997.00049.x;
RA Gerike U., Danson M.J., Russell N.J., Hough D.W.;
RT "Sequencing and expression of the gene encoding a cold-active citrate
RT synthase from an Antarctic bacterium, strain DS2-3R.";
RL Eur. J. Biochem. 248:49-57(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=DS2-3R;
RX PubMed=9579066; DOI=10.1099/00221287-144-4-929;
RA Gerike U., Hough D.W., Russell N.J., Dyall-Smith M.L., Danson M.J.;
RT "Citrate synthase and 2-methylcitrate synthase: structural, functional and
RT evolutionary relationships.";
RL Microbiology 144:929-935(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 2-379 IN COMPLEX WITH COENZYME A
RP AND SUBSTRATE, ACTIVE SITE, AND SUBUNIT.
RC STRAIN=DS2-3R;
RX PubMed=9551556; DOI=10.1016/s0969-2126(98)00037-9;
RA Russell R.J., Gerike U., Danson M.J., Hough D.W., Taylor G.L.;
RT "Structural adaptations of the cold-active citrate synthase from an
RT Antarctic bacterium.";
RL Structure 6:351-361(1998).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and via the
CC 2-methylcitrate cycle I (propionate degradation route). Catalyzes the
CC Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield
CC 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of
CC oxaloacetate with acetyl-CoA but with a lower specificity.
CC {ECO:0000269|PubMed:9310359, ECO:0000269|PubMed:9579066}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate +
CC CoA + H(+); Xref=Rhea:RHEA:23780, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:58853; EC=2.3.3.5;
CC Evidence={ECO:0000269|PubMed:9579066};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000269|PubMed:9310359,
CC ECO:0000269|PubMed:9579066};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for oxaloacetate (with propionyl-CoA at pH 8 and 23 degrees
CC Celsius) {ECO:0000269|PubMed:9579066};
CC KM=6.9 uM for oxaloacetate (with acetyl-CoA at pH 8 and 23 degrees
CC Celsius) {ECO:0000269|PubMed:9310359};
CC KM=7 uM for oxaloacetate (with acetyl-CoA at pH 8 and 23 degrees
CC Celsius) {ECO:0000269|PubMed:9579066};
CC KM=16 uM for propionyl-CoA (at pH 8 and 23 degrees Celsius)
CC {ECO:0000269|PubMed:9579066};
CC KM=229 uM for acetyl-CoA (at pH 8 and 23 degrees Celsius)
CC {ECO:0000269|PubMed:9579066};
CC KM=230 uM for acetyl-CoA (at pH 8 and 23 degrees Celsius)
CC {ECO:0000269|PubMed:9310359};
CC Vmax=12 umol/min/mg enzyme with propionyl-CoA as substrate (at pH 8
CC and 23 degrees Celsius) {ECO:0000269|PubMed:9579066};
CC Vmax=30 umol/min/mg enzyme with acetyl-CoA as substrate (at pH 8 and
CC 23 degrees Celsius) {ECO:0000269|PubMed:9310359,
CC ECO:0000269|PubMed:9579066};
CC Note=kcat is 8 sec(-1) for 2-methylcitrate synthase activity with
CC propionyl-CoA as substrate (at pH 8 and 23 degrees Celsius). kcat is
CC 21 sec(-1) for citrate synthase activity with acetyl-CoA as substrate
CC (at pH 8 and 23 degrees Celsius). {ECO:0000269|PubMed:9310359,
CC ECO:0000269|PubMed:9579066};
CC Temperature dependence:
CC Optimum temperature is 31 degrees Celsius. Cold-active. Is rapidly
CC inactivated at 45 degrees Celsius, and shows significant activity at
CC 10 degrees Celsius and below. {ECO:0000269|PubMed:9310359};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:9579066}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2. {ECO:0000305|PubMed:9579066}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9310359,
CC ECO:0000269|PubMed:9551556}.
CC -!- INDUCTION: By growth on propionate, but not acetate or glucose.
CC {ECO:0000269|PubMed:9579066}.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; U85944; AAC45662.1; -; Genomic_DNA.
DR PDB; 1A59; X-ray; 2.09 A; A=2-379.
DR PDBsum; 1A59; -.
DR AlphaFoldDB; O34002; -.
DR SMR; O34002; -.
DR DrugBank; DB04272; Citric acid.
DR DrugBank; DB01992; Coenzyme A.
DR PRIDE; O34002; -.
DR BRENDA; 2.3.3.1; 15675.
DR SABIO-RK; O34002; -.
DR UniPathway; UPA00223; UER00717.
DR UniPathway; UPA00946; -.
DR EvolutionaryTrace; O34002; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:UniProtKB.
DR GO; GO:0036440; F:citrate synthase activity; IDA:UniProtKB.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR024176; Citrate_synthase_bac-typ.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01800; cit_synth_II; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Transferase;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9310359"
FT CHAIN 2..379
FT /note="2-methylcitrate synthase"
FT /id="PRO_0000169925"
FT ACT_SITE 222
FT /evidence="ECO:0000269|PubMed:9551556"
FT ACT_SITE 270
FT /evidence="ECO:0000269|PubMed:9551556"
FT ACT_SITE 321
FT /evidence="ECO:0000269|PubMed:9551556"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 264..268
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:9551556"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9551556"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9551556"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1A59"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1A59"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1A59"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:1A59"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 117..142
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:1A59"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:1A59"
FT TURN 220..224
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 244..260
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 298..314
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1A59"
FT HELIX 338..359
FT /evidence="ECO:0007829|PDB:1A59"
SQ 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
