CISY_EMENI
ID CISY_EMENI Reviewed; 474 AA.
AC O00098; C8V3P7; Q5ATV5; Q8NKF2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Citrate synthase, mitochondrial;
DE EC=2.3.3.16;
DE Flags: Precursor;
GN Name=citA; ORFNames=AN8275;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=9163747;
RA Park B.W., Han K.H., Lee C.Y., Lee C.H., Maeng P.J.;
RT "Cloning and characterization of the citA gene encoding the mitochondrial
RT citrate synthase of Aspergillus nidulans.";
RL Mol. Cells 7:290-295(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RA Seo S.W., Lee C.H., Maeng P.J.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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.
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; U89675; AAC49728.3; -; Genomic_DNA.
DR EMBL; AF468824; AAM22645.1; -; mRNA.
DR EMBL; AACD01000145; EAA59013.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF74260.1; -; Genomic_DNA.
DR RefSeq; XP_681544.1; XM_676452.1.
DR AlphaFoldDB; O00098; -.
DR SMR; O00098; -.
DR STRING; 162425.CADANIAP00004335; -.
DR PRIDE; O00098; -.
DR EnsemblFungi; CBF74260; CBF74260; ANIA_08275.
DR EnsemblFungi; EAA59013; EAA59013; AN8275.2.
DR GeneID; 2868998; -.
DR KEGG; ani:AN8275.2; -.
DR VEuPathDB; FungiDB:AN8275; -.
DR eggNOG; KOG2617; Eukaryota.
DR HOGENOM; CLU_022049_2_1_1; -.
DR InParanoid; O00098; -.
DR OMA; TVGWCAQ; -.
DR OrthoDB; 1131452at2759; -.
DR BRENDA; 2.3.3.16; 517.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:AspGD.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IMP:AspGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISA:AspGD.
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; Reference proteome; Transferase; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..474
FT /note="Citrate synthase, mitochondrial"
FT /id="PRO_0000005477"
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"
FT CONFLICT 167
FT /note="C -> V (in Ref. 1; AAC49728 and 3; AAM22645)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="Y -> T (in Ref. 1; AAC49728 and 3; AAM22645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 52227 MW; 2CA133032DE5C3EC CRC64;
MASTLRLSTS ALRSSTLAGK PVVQSVAFNG LRCYSTGKTK SLKETFADKL PGELEKVKKL
RKEHGNKVIG ELTLDQAYGG ARGVKCLVWE GSVLDSEEGI RFRGLTIPEC QKLLPKAPGG
EEPLPEGLFW LLLTGEVPSE QQVRDLSAEW AARSDLPKFI EELIDRCPST LHPMAQFSLA
VTALEHESAF AKAYAKGINK KEYWHYTFED SMDLIAKLPT IAAKIYRNVF KDGKVAPIQK
DKDYSYNLAN QLGFADNKDF VELMRLYLTI HSDHEGGNVS AHTTHLVGSA LSSPMLSLAA
GLNGLAGPLH GLANQEVLNW LTEMKKVVGN DLSDQSIKDY LWSTLNAGRV VPGYGHAVLR
KTDPRYTSQR EFALRKLPDD PMFKLVSQVY KIAPGVLTEH GKTKNPYPNV DAHSGVLLQY
YGLTEANYYT VLFGVSRALG VLPQLIIDRA FGAPIERPKS FSTEAYAKLV GAKL
