ID S8A7K4_DACHA Unreviewed; 472 AA.
AC S8A7K4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN ORFNames=H072_7287 {ECO:0000313|EMBL:EPS38980.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS38980.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS38980.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS38980.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EPS38980.1}.
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DR EMBL; AQGS01000513; EPS38980.1; -; Genomic_DNA.
DR RefSeq; XP_011113049.1; XM_011114747.1.
DR AlphaFoldDB; S8A7K4; -.
DR STRING; 1284197.S8A7K4; -.
DR eggNOG; KOG2617; Eukaryota.
DR HOGENOM; CLU_022049_2_1_1; -.
DR OMA; VLEWLFK; -.
DR OrthoDB; 3513214at2759; -.
DR Proteomes; UP000015100; 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:UP000015100};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000441}.
FT ACT_SITE 308
FT /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
FT ACT_SITE 354
FT /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
FT ACT_SITE 409
FT /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
SQ SEQUENCE 472 AA; 52061 MW; 5E866BE4A125D0C5 CRC64;
MASLRIASTA LRSAARPAFS STRSVGFNAL RCYSSTGKSL KETFAEKVPQ EIEKIKKLKK
EHGSKVLGEV TLEQVYGGAR GIKSLVWEGS VLDAEEGIRF RGKTIPECQE VLPKAEGGEE
PLPEGLFWLL LTGEVPTTEQ VRGLSAEWAA RAELPKFIEE LIDRCPTDLH PMAQFSLAVT
ALEHQSSFAK AYAKGINKKD YWTYAFEDSM DLIGKLPTIA SRIYQNVFKG GKHVPVQKDK
DYGYNLANML GYGENKDFVE LMRLYLTIHS DHEGGNVSAH TTHLVGSALS SPMLSFAAGL
NGLAGPLHGL ANQEVLNWLF KMKEKIGNDL SDKAITDYLW STLNAGQVVP GYGHAVLRKT
DPRYVSQREF ALKKLPEDPM FKLVSQVYKI APGVLTEHGK TKNPYPNVDA HSGVLLQYYG
MTEANFYTVL FGVSRALGVL PQLIIDRAVG MPIERPKSFS TEKYAKLVGA TL
//
