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Database: UniProt
Entry: H1UVB0_COLHI
LinkDB: H1UVB0_COLHI
Original site: H1UVB0_COLHI 
ID   H1UVB0_COLHI            Unreviewed;       471 AA.
AC   H1UVB0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN   ORFNames=CH063_04398 {ECO:0000313|EMBL:CCF31911.1}, CH63R_06953
GN   {ECO:0000313|EMBL:OBR08188.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF31911.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|EMBL:CCF31911.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:CCF31911.1};
RA   Ma L.-J., O'Connell R., van Themaat E.V.L., Stueber K., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Colletotrichum higginsianum IMI 34906.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
RN   [3] {ECO:0000313|EMBL:OBR08188.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:OBR08188.1};
RA   O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT   "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000092177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX   PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA   Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA   Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA   Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA   Thon M.R., O'Connell R.J.;
RT   "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT   structure and association of transposable elements with secondary
RT   metabolite gene clusters.";
RL   BMC Genomics 18:667-667(2017).
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; CACQ02000267; CCF31911.1; -; Genomic_DNA.
DR   EMBL; LTAN01000005; OBR08188.1; -; Genomic_DNA.
DR   RefSeq; XP_018156706.1; XM_018301928.1.
DR   STRING; 759273.H1UVB0; -.
DR   EnsemblFungi; CCF31911; CCF31911; CH063_04398.
DR   GeneID; 28866035; -.
DR   KEGG; chig:CH63R_06953; -.
DR   VEuPathDB; FungiDB:CH63R_06953; -.
DR   eggNOG; KOG2617; Eukaryota.
DR   HOGENOM; CLU_022049_2_1_1; -.
DR   OrthoDB; 3513214at2759; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   Proteomes; UP000092177; Chromosome 5.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0050440; F:2-methylcitrate synthase activity; IEA:EnsemblFungi.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:EnsemblFungi.
DR   GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:EnsemblFungi.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:EnsemblFungi.
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; IPR010109; Citrate_synthase_euk.
DR   InterPro; IPR036969; Citrate_synthase_sf.
DR   NCBIfam; TIGR01793; cit_synth_euk; 1.
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}.
FT   ACT_SITE        306
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
FT   ACT_SITE        352
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
FT   ACT_SITE        409
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
SQ   SEQUENCE   471 AA;  51938 MW;  F189A5370F456957 CRC64;
     MNVTRSTRAL GALRPLAARS ALNVRQYSSS SESDLKTTLK SVIPAKRELL KKVKAHSSKV
     IGEVKVENAL GGMRGLKAMV WEGSVLDANE GIRFHGKTIK DCQKELPKGK TGTEMLPEAM
     FWLLLTGQVP STNQVRQFSR ELAEQAQLPD FVNELLDNFP TDLHPMTQFA IAVSALNYTS
     KFAKAYEQGL NKADYWEPTF DDSISLLAKL PTIAAKIYQN SYRGGGALPA EVDLEQDWSY
     NFAAMLGKGG KENENFQDLL RLYLALHGDH EGGNVSAHTT HLVGSALSDP FLSYSAGLQG
     LAGPLHGLAA QEVLRWIIQM KDNIPKSYTD KDVTDYLWST LNSGRVVPGY GHAVLRKPDP
     RFEALMDYAA ARPEIAQDPV FQLVQKNSQI APEVLKKHGK TKNPYPNVDS SSGVLFHHYG
     FHETLYYTAT FGVSRGLGPL AQLIWDRALG LPIERPKSIN LEGLLKQAES S
//
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