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Database: UniProt
Entry: A0A0D6ZZQ8_9AGAR
LinkDB: A0A0D6ZZQ8_9AGAR
Original site: A0A0D6ZZQ8_9AGAR 
ID   A0A0D6ZZQ8_9AGAR        Unreviewed;       431 AA.
AC   A0A0D6ZZQ8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-NOV-2023, entry version 24.
DE   RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN   ORFNames=FISHEDRAFT_68219 {ECO:0000313|EMBL:KIY43033.1};
OS   Fistulina hepatica ATCC 64428.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX   NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY43033.1, ECO:0000313|Proteomes:UP000054144};
RN   [1] {ECO:0000313|EMBL:KIY43033.1, ECO:0000313|Proteomes:UP000054144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY43033.1,
RC   ECO:0000313|Proteomes:UP000054144};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
CC   -!- SIMILARITY: Belongs to the citrate synthase family.
CC       {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|RuleBase:RU000441}.
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DR   EMBL; KN882143; KIY43033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D6ZZQ8; -.
DR   OrthoDB; 3513214at2759; -.
DR   Proteomes; UP000054144; Unassembled WGS sequence.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:InterPro.
DR   GO; GO:0006101; P:citrate metabolic process; 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; 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:SF8; CITRATE SYNTHASE, 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:UP000054144};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000441}.
FT   ACT_SITE        267
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
FT   ACT_SITE        313
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
FT   ACT_SITE        368
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
SQ   SEQUENCE   431 AA;  47390 MW;  3BA05A3D7A2CD1B3 CRC64;
     MFAARSASFK HAVKAVRSEH GQKAFGPVIV DQLYGGMRGL PALIWDGSVL DAEEGIRFRD
     RTIPEIQEAL PSAPGGTEPL PEGLFWLLLT GEIPTNEQVT QLSKLFAQHS ALPEFVEKLI
     DTCPTTLHPM SQFSLAVTAL NHDSAFAKAY HEGIHKRDYW DPTFDDAINL IAKLPAIAGR
     IYNNVYRNRK ATPAIDASKD YAWNLSHLLG FSDNEAFNEL MRLYITIHSD HEGGNVSAHT
     GKLVGSALSD PFLAFAASLN GLAGPLHGLA NQEVLVWVTK MQESIGADAS DDAVREYVWS
     TLKGGKVVPG YGHAVLRKTD PRYVAQREFA LKHMPNDKLF KLVSQLYTIV PKVLLEAGKA
     KNPWPNVDAH SGVLLTYYGL TEMNYYTVLF GVSRAFGVAA QLIWDRALGA PLERPKSYST
     AAIAKMFANR S
//
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