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Database: UniProt
Entry: K2R6V6_MACPH
LinkDB: K2R6V6_MACPH
Original site: K2R6V6_MACPH 
ID   K2R6V6_MACPH            Unreviewed;       479 AA.
AC   K2R6V6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN   ORFNames=MPH_04741 {ECO:0000313|EMBL:EKG18051.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG18051.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG18051.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG18051.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKG18051.1}.
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DR   EMBL; AHHD01000218; EKG18051.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2R6V6; -.
DR   STRING; 1126212.K2R6V6; -.
DR   VEuPathDB; FungiDB:MPH_04741; -.
DR   eggNOG; KOG2617; Eukaryota.
DR   HOGENOM; CLU_022049_2_1_1; -.
DR   InParanoid; K2R6V6; -.
DR   OrthoDB; 3513214at2759; -.
DR   Proteomes; UP000007129; 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:UP000007129};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000441}.
FT   REGION          22..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  52437 MW;  DD815CBE2E11C88C CRC64;
     MALNARTASR AFRSVRPSAI KTAASVQPRE PSRSYASSSE PGLKETLARV IPAKRELLKK
     VKAHADKSIG EVKVENTLGG MRGLKAMVWE GSVLDANEGI RFHGRTIKDC QAQLPKGTSG
     TEMLPEAMFW LLLTGEVPTT SQVRKLSREL AEKAAIPAFV SKMLDDFPKD LHPMTQFACA
     VSALNYESKF AKKYEQGLNK ADYWEPTYDD VISLLAKLPT IAAKIYQNAY RGGGSLPAEV
     DVNQDWSYNF AAMLGKGGKE NEGFQDLLRL YLALHGDHEG GNVSAHATHL VGSALSDPFL
     SYSAGLQGLA GPLHGLAAQE VLRWILQMKE AIPNDFTESH IKDYLWTTLK SGRVIPGYGH
     AVLRKPDPRF QALMDFAAAR PEIANDPVFR LVKANSDIAP QVLTEHGKTK NPFPNVDSSS
     GVLFHYYGFK ETLYYTATFG VSRGLGPLAQ LIWDRALGLP IERPKSINLE GILKQVGGA
//
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