ID A0A165EUJ4_9APHY Unreviewed; 492 AA.
AC A0A165EUJ4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369, ECO:0000256|RuleBase:RU000441};
GN ORFNames=LAESUDRAFT_724785 {ECO:0000313|EMBL:KZT07791.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT07791.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT07791.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT07791.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2. {ECO:0000256|ARBA:ARBA00004751}.
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|PIRNR:PIRNR001369,
CC ECO:0000256|RuleBase:RU000441}.
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DR EMBL; KV427618; KZT07791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EUJ4; -.
DR STRING; 1314785.A0A165EUJ4; -.
DR InParanoid; A0A165EUJ4; -.
DR OrthoDB; 642531at2759; -.
DR Proteomes; UP000076871; 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; IPR024176; Citrate_synthase_bac-typ.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR42871; CITRATE SYNTHASE; 1.
DR PANTHER; PTHR42871:SF1; CITRATE SYNTHASE; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 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:UP000076871};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001369};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT ACT_SITE 334
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 390
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 492 AA; 54879 MW; 99D27894D493E2CD CRC64;
MGKLPATSEN TLTVRDNRTG KTYSIPIVDN AAPATAFKKI TAPRKANERE ENETERGLRI
EDKGFLNTAV IRSQITYIDG EAGVLRYRGY PIEQLALHSN HLETAYLLIY GNLPTKEQFA
FFQSEVMRHG PTHADSEQFF RSFRYDAHPM SMLTSAFAML GSFYAEANPS LQGQRLYTRG
DKESLAVMDR QIYRLIGKAT TLAAMAYRVR QGRDFVSPPA GLSYTGSFLY QMDHLGEENY
VPNPVLEKAL DVLFLIHADH ELNASCTTVL QTASSLVDPY SAIAAGCASL YGPLHGGANE
AVIRMLISIG SPENVPAFIE AVKRREKTLS GFGHRVYKTS DPRSFIVRKT ADEVFKVTGK
DELLVTAMAL HDAAMKDEYF ISRKLAPNVD FCSGLIYRAM GFPMDFFPVL FVVPRVVGWL
AHWRQMMLQD GGVKIWRPRQ VYAGPGQRDF VPVDERVVVK GPGQTPSVVE HGGITKRTML
ATFTGKRMPS RL
//
