ID A0A0J7BGS0_COCIT Unreviewed; 473 AA.
AC A0A0J7BGS0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN ORFNames=CIRG_09637 {ECO:0000313|EMBL:KMP09467.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP09467.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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:0000256|ARBA:ARBA00036244};
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000308};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005026}.
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|RuleBase:RU000441}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS028099; KMP09467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7BGS0; -.
DR STRING; 404692.A0A0J7BGS0; -.
DR Proteomes; UP000054565; Unassembled WGS sequence.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1.
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; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR PANTHER; PTHR11739:SF15; CITRATE SYNTHASE 3, MITOCHONDRIAL; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; Citrate synthase; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000441}.
SQ SEQUENCE 473 AA; 51788 MW; A2EA4F7EBBB23BB7 CRC64;
MALAARASRQ ALRAAKASSS RTVAGSSRSY ASAAESELKS VFRSVLPAKR ALLKELKEHN
DAKIGDVTVA NAIGGMRGLK AMIWEGSVLD PEEGIRFHGH TIKDCQQMLP KGTSGTEMLP
EAMFWLLLTG QVPTTPQIRA FSRELAEKSH LPKHILDMIK SFPKDMHPMT QLSVAVAALN
TESTFAKKYA EGLNKADYWE PTFDDSISLL AKIPRVAALV FRPNEVDTVG TQQLDSTQDW
AYNFAVLLGK GGKEHESFHD VLRLYLALHG DHEGGNVSAH ATHLVGSALS DPFLSYSAGL
LGLAGPLHGL AAQEVLRWIL NMRAKIGDNF TEKDVKDYLW STLKSGQVVP GYGHGVLRKP
DPRFEALMDF ASTRPEIMNN PVFKLVKKNS EIAPGVLTEH GKTKNPHPNV DAASGVLFHH
YGFQEPLYYT VTFGVSRALG PLAQLIWSRA LGLPIERPKS INMQGLLNSV KKN
//
