ID G3JGY2_CORMM Unreviewed; 736 AA.
AC G3JGY2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN ORFNames=CCM_05696 {ECO:0000313|EMBL:EGX91538.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX91538.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX91538.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX91538.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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}.
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DR EMBL; JH126402; EGX91538.1; -; Genomic_DNA.
DR RefSeq; XP_006670903.1; XM_006670840.1.
DR AlphaFoldDB; G3JGY2; -.
DR STRING; 983644.G3JGY2; -.
DR GeneID; 18167714; -.
DR KEGG; cmt:CCM_05696; -.
DR VEuPathDB; FungiDB:CCM_05696; -.
DR eggNOG; KOG2617; Eukaryota.
DR HOGENOM; CLU_022049_2_0_1; -.
DR InParanoid; G3JGY2; -.
DR OrthoDB; 3513214at2759; -.
DR Proteomes; UP000001610; 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; 2.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; Citrate synthase; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000441}.
FT REGION 75..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 81064 MW; 5E2DBEE0C30FC058 CRC64;
MVVGTPATWQ ASVLSDSAKI GGCPGGFGWS TRLYSPSGSR SGCRWPQVQS LSPSKRKWIG
NAHVRVRFAR PSAPARRAAY KEPGEVLRDE LEDDENPTSK LTAEATVGEM ANCLKRRKIR
AKTWPQPLAN CVRRSAGFPR LCLAPTKIRV AEPTPGSLRP GRAHGGHWHS GEREKKVSHT
LTERDFISFP PPYLFFIIVN HPVSAQPCPH RTDHRLTPRF SSPEIEIAAS SLVLVPTRTI
YNQHIMAMNL RTSARAIGSF KPLARAALGG ARAYATAEPD LKATLKAAIP EKRELLKKVR
AHGDKVIGEV KVENTLGGMR GLKAMVWEGS VLDANEGIRF HGRTIKECQQ ALPKGTSGTE
MLPEAMFWLL LTGQVPSVAQ VRVFSRELAE QAAIPAFVSK MLDDFPRDLH PMTQFAMAVS
ALNYESKFAK AYEKGLNKAD YWEPTFDDSI SLLAKLPTIA AKIYQNAYKG GGALPAEVDL
NQDWSYNYAA LLGKGGKENE NFQDLLRLYL ALHGDHEGGN VSAHATHLVG SALSDPFLSY
SAGLQGLAGP LHGYVALIQK KGEKKRLTLY YSLAAQEVLR WILQMKENIP ADHTEKDVED
YLWSTLNSGR VVPGYGHAVL RKPDPRFEAL MDYAAARPEI AADPVFQLVE KNSRIAPEVL
KKHGKTKNPY PNVDSSSGVL FHHYGFHETL YYTATFGVSR GLGPLAQLIW DRALGLPIER
PKSINLAGLL KQVEGN
//
