ID A0A161VPZ7_9PEZI Unreviewed; 489 AA.
AC A0A161VPZ7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=ATP citrate synthase {ECO:0000256|ARBA:ARBA00012639};
DE EC=2.3.3.8 {ECO:0000256|ARBA:ARBA00012639};
GN ORFNames=CI238_04319 {ECO:0000313|EMBL:KZL79214.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL79214.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL79214.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL79214.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate +
CC CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001688};
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:KZL79214.1}.
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DR EMBL; LFIW01002127; KZL79214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161VPZ7; -.
DR STRING; 1573173.A0A161VPZ7; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.30.470.110; -; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR032263; Citrate-bd.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR23118:SF57; ATP CITRATE SYNTHASE; 1.
DR PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF16114; Citrate_bind; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 73..228
FT /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT /evidence="ECO:0000259|Pfam:PF08442"
FT DOMAIN 298..474
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
SQ SEQUENCE 489 AA; 53299 MW; 30A0BFE2CD7684B6 CRC64;
MSAKSILEAD GKAILNYHLT RAPVIKPTPL PTPTKHNPPP RLCSLHFPED ANVEDVLNQA
EVTYPWVLQP GTKFVAKPDQ LIKRRGKSGL LALNKTWAEA RAWIAERAGK EVKVETTTGV
LRQFLVEPFV PHPQDTEYYI NIMSVRDGDW ILFTHEGGVD VGDVDAKAEK LLIPVDLSQY
PSNDEIAATL LKKVPKGVHN VLVDFISRLY AVYVECQFTY LEINPLVVIP NEDATSASVH
FLDLAAKLDQ TADFECGVKW AIARSPAALG LTNVAASNGE KVNIDAGPPM EFPAPFGREL
TKEEAYIADL DAKTGASLKL TVLNPNGRIW TLVAGGGASV VYADAIASSG FADELANYGE
YSGAPTESQT YHYARTVLDL MLRAPLSEQG KVLFIGGGIA NFTNVASTFK GVIRALRDYA
KQLNEHNVQI WVRRAGPNYQ EGLKNMKAAT QELGLNAKIF GPEMHVSGIV PLALVPGRWE
ASGAEEFRG
//
