ID A2R4X3_ASPNC Unreviewed; 465 AA.
AC A2R4X3;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN ORFNames=An15g01920 {ECO:0000313|EMBL:CAK42295.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK42295.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK42295.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270337; CAK42295.1; -; Genomic_DNA.
DR RefSeq; XP_001396731.1; XM_001396694.2.
DR AlphaFoldDB; A2R4X3; -.
DR EnsemblFungi; CAK42295; CAK42295; An15g01920.
DR GeneID; 4987793; -.
DR KEGG; ang:An15g01920; -.
DR VEuPathDB; FungiDB:An15g01920; -.
DR HOGENOM; CLU_022049_2_0_1; -.
DR OrthoDB; 3513214at2759; -.
DR Proteomes; UP000006706; Chromosome 3R.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:AspGD.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:EnsemblFungi.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IDA:AspGD.
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; 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 Acyltransferase {ECO:0000313|EMBL:CAK42295.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000441}.
SQ SEQUENCE 465 AA; 51267 MW; 617E1BEF277338EC CRC64;
MSFSMPIRPT TRHASRLAQA KIRSGRLYST ESDLKTALKS VIPEKRELFK QVKARSDDVV
GEVKVGNIIG GMRGLKSMLW EGSVLDPEEG IRFHGKTIKD CQRELPKGTT GTEMLPEAMF
WLLLTGQVPT TSQVRAFSRE LAEKSHLPDH ILGLIKLFPK DMHPMTQLSV AVAALNTEST
FAKAYERGLN KADYWEPTFD DSISLLAKIP RVAALVFRSN EIDQVGTQAL DATQDWSHNF
AELLGKGGAE HADFHDLLRL YLALHGDHEG GNVSAHATHL VGSALSDPFL SYSAGLLGLA
GPLHGLAAQE VLRWILAMQE KIGTQVTDDS VRTYLWDTLK SGRVVPGYGH GVLRKPDPRF
EALMDFAATR PDVQANPVFQ LVKKNSEIAP EVLTQHGKTK NPHPNVDAAS GVLFYHYGFQ
QPLYYTVTFG VSRALGPLVQ LIWDRALGLP IERPKSINLK GLIGN
//
