ID K1WFN2_MARBU Unreviewed; 473 AA.
AC K1WFN2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN ORFNames=MBM_05564 {ECO:0000313|EMBL:EKD16270.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16270.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD16270.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16270.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|RuleBase:RU000441}.
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DR EMBL; JH921439; EKD16270.1; -; Genomic_DNA.
DR RefSeq; XP_007293453.1; XM_007293391.1.
DR AlphaFoldDB; K1WFN2; -.
DR STRING; 1072389.K1WFN2; -.
DR GeneID; 18761499; -.
DR KEGG; mbe:MBM_05564; -.
DR eggNOG; KOG2617; Eukaryota.
DR HOGENOM; CLU_022049_2_1_1; -.
DR InParanoid; K1WFN2; -.
DR OMA; VLEWLFK; -.
DR OrthoDB; 3513214at2759; -.
DR Proteomes; UP000006753; 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 CDD; cd06105; ScCit1-2_like; 1.
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:UP000006753};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000441}.
FT ACT_SITE 309
FT /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
FT ACT_SITE 355
FT /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
SQ SEQUENCE 473 AA; 52059 MW; D7E37EEFD4523AD8 CRC64;
MSSALRIGSS ALRSSITAQT FAKTTAFTGL RFYSASKSQT LKERFAEQLP EKIEQIKKLR
KDYGSKVVGE VTLDQVYGGA RGIKSLVWEG SVLDSEEGIR FRGKTIPECQ ELLPKAPGGK
EPLPEGLFWL LLTGEVPSEQ QVRDLSADWA ARAEIPKFVE ELIDRCPNDL HPMAQFSIAV
NALEHESAFA KAYAKGMKKS EYWGHTFEDS MDLIAKLPTI AARIYQNVFK GGKVAPVQKD
KDYSFNFANQ LGFADNHDFV ELMRLYLTIH TDHEGGNVSA HTTHLVGSAL SSPMLSLAAG
LNGLAGPLHG LANQEVLNWL TKMKAAIGDD LSDKAITDYL WSTLKAGQVV PGYGHAVLRK
TDPRYMAQRT FAESHLPNDP MYKLVSQVYK IAPGVLTEHG KTKNPFPNVD AHSGVLLQYY
GLTEANYYTV LFGVSRAIGV LPQLIIDRAV GAPIERPKSF STEKWAEIVG AKL
//
