ID A0A177E357_ALTAL Unreviewed; 471 AA.
AC A0A177E357;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN ORFNames=CC77DRAFT_1005031 {ECO:0000313|EMBL:OAG25419.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG25419.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG25419.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG25419.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441470; OAG25419.1; -; Genomic_DNA.
DR RefSeq; XP_018390840.1; XM_018523317.1.
DR AlphaFoldDB; A0A177E357; -.
DR STRING; 5599.A0A177E357; -.
DR GeneID; 29108911; -.
DR KEGG; aalt:CC77DRAFT_1005031; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1005031; -.
DR OMA; IDHGFNA; -.
DR OrthoDB; 3513214at2759; -.
DR Proteomes; UP000077248; 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 Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000441}.
SQ SEQUENCE 471 AA; 51650 MW; 4768F4A9B2D36A2D CRC64;
MALSARSASR ALRAAKGRPF ASVQACSYSS SSEPDLKETF KKVLPAKREL LKKVKAHADK
KLGDVKVENA LGGMRGLKAM VWEGSVLDAN EGIRFHGKTI KDCQKVLPKG TSGTEMLPEA
MFWLLLTGEV PSVSQTRALS RELAEKGSIP KFVEKMLDDF PKDLHPMTQF ACAVSALNYE
SKFAKAYEKG INKADYWEPT FDDCISLLAK LPTIAAKIYQ NAYRGGGALP NEIDLNQDWS
YNFAAMLGKP GKENEGFQDL LRLYLALHGD HEGGNVSAHT THLVGSALSD PFLSYSAGLQ
GLAGPLHGLA AQEVLRFILD MQKVVGEKFT EKDVNEYLWS VLKSGRVIPG YGHAVLRKPD
PRFEALMDFA NARPEIAANP VYQLVKKNSE VAPDVLKEHG KTKNPFPNVD SSSGVLFHHY
GFQETLYYTA TFGVSRGLGP LAQLIWDRAL GLPIERPKSI NLQGILDQVG A
//
