ID G7XMX9_ASPKW Unreviewed; 474 AA.
AC G7XMX9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN ORFNames=AKAW_06279 {ECO:0000313|EMBL:GAA88165.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA88165.1};
RN [1] {ECO:0000313|EMBL:GAA88165.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA88165.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|RuleBase:RU000441}.
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DR EMBL; DF126462; GAA88165.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XMX9; -.
DR STRING; 1033177.G7XMX9; -.
DR VEuPathDB; FungiDB:AKAW_06279; -.
DR eggNOG; KOG2617; Eukaryota.
DR InParanoid; G7XMX9; -.
DR Proteomes; UP000006812; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000441}.
FT ACT_SITE 310
FT /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
FT ACT_SITE 356
FT /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
FT ACT_SITE 411
FT /evidence="ECO:0000256|PIRSR:PIRSR610109-1"
SQ SEQUENCE 474 AA; 52026 MW; 868CB713CEB485C1 CRC64;
MASTLRLGTS ALRTSSIAAK PVVQSAAFNG LRCYSTGKAK SLKETFAEKL PAELEKVKKL
RKEHGSKVIG EVTLDQAYGG ARGVKCLVWE GSVLDSEEGI RFRGRTIPEC QELLPKAPGG
QEPLPEGLFW LLLTGEIPTE QQVRDLSAEW AARSDLPKFI EELIDRCPST LHPMSQFSLA
VTALEHESAF AKAYAKGINK KDYWNYTFED SMDLIAKLPT IAAKIYRNVF KDGKVAPIQK
DKDYSYNLAN QLGYGDNNDF VELMRLYLTI HSDHEGGNVS AHTTHLVGSA LSSPMLSLAA
GLNGLAGPLH GLANQEVLNW LTKMKAAIGN DLSDEAIKNY LWSTLNAGQV VPGYGHAVLR
KTDPRYVSQR EFALRKLPDD PMFKLVSQVY KIAPGVLTEH GKTKNPYPNV DAHSGVLLQY
YGLTEANYYT VLFGVSRALG VLPQLIIDRA LGAPIERPKS YSTEAFAKLV GAKL
//