CISY_ASPNG
ID CISY_ASPNG Reviewed; 475 AA.
AC P51044;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Citrate synthase, mitochondrial;
DE EC=2.3.3.16;
DE Flags: Precursor;
GN Name=cit-1;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=WU-2223L;
RA Oshida Y., Miyake K., Kanayama S., Kirimura K., Usami S.;
RT "Cloning and expression of cDNA encoding Aspergillus niger citrate synthase
RT in Esherichia coli.";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10117};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC oxidative metabolism.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; D63376; BAA09691.1; -; mRNA.
DR AlphaFoldDB; P51044; -.
DR SMR; P51044; -.
DR STRING; 5061.CADANGAP00008062; -.
DR PRIDE; P51044; -.
DR VEuPathDB; FungiDB:An09g06680; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1141371; -.
DR VEuPathDB; FungiDB:ATCC64974_7730; -.
DR VEuPathDB; FungiDB:M747DRAFT_318975; -.
DR eggNOG; KOG2617; Eukaryota.
DR UniPathway; UPA00223; UER00717.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:UniProtKB-UniPathway.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 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 PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01793; cit_synth_euk; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 2: Evidence at transcript level;
KW Mitochondrion; Transferase; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..475
FT /note="Citrate synthase, mitochondrial"
FT /id="PRO_0000005475"
FT ACT_SITE 310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ SEQUENCE 475 AA; 52154 MW; F93525B3F31FCB3F CRC64;
MASTLRLGTS ALRSSSIAAK 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 YSTELSPSLL VLSCK
