CISY_THEAC
ID CISY_THEAC Reviewed; 385 AA.
AC P21553;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Citrate synthase;
DE EC=2.3.3.16;
GN Name=gltA; OrderedLocusNames=Ta0169;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=2269303; DOI=10.1111/j.1432-1033.1990.tb19477.x;
RA Sutherland K.J., Henneke C.M., Towner P., Hough D.W., Danson M.J.;
RT "Citrate synthase from the thermophilic archaebacterium Thermoplasma
RT acidophilium. Cloning and sequencing of the gene.";
RL Eur. J. Biochem. 194:839-844(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [3]
RP PROTEIN SEQUENCE OF 2-17.
RA Smith L.D., Stevenson K.J., Hough D.W., Danson M.J.;
RT "Citrate synthase from the thermophilic archaebacteria Thermoplasma
RT acidophilum and Sulfolobus acidocaldarius.";
RL FEBS Lett. 225:277-281(1987).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=7704526; DOI=10.1016/s0969-2126(94)00118-9;
RA Russel R.J.M., Hough D.W., Danson M.J., Taylor G.L.;
RT "The crystal structure of citrate synthase from the thermophilic archaeon,
RT Thermoplasma acidophilum.";
RL Structure 2:1157-1167(1994).
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 -!- ACTIVITY REGULATION: Allosterically inhibited by NADH.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homodimer.
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; X55282; CAA38996.1; -; Genomic_DNA.
DR EMBL; AL445063; CAC11315.1; -; Genomic_DNA.
DR PIR; S13831; YKYT.
DR RefSeq; WP_010900596.1; NC_002578.1.
DR PDB; 2IFC; X-ray; 1.70 A; A/B/C/D=1-385.
DR PDB; 2R26; X-ray; 2.50 A; A/B/C/D=2-385.
DR PDB; 2R9E; X-ray; 1.95 A; A/B/C/D=1-385.
DR PDB; 4YBO; X-ray; 2.18 A; A/B/C/D=2-385.
DR PDBsum; 2IFC; -.
DR PDBsum; 2R26; -.
DR PDBsum; 2R9E; -.
DR PDBsum; 4YBO; -.
DR AlphaFoldDB; P21553; -.
DR SMR; P21553; -.
DR STRING; 273075.Ta0169; -.
DR PRIDE; P21553; -.
DR EnsemblBacteria; CAC11315; CAC11315; CAC11315.
DR GeneID; 1455814; -.
DR KEGG; tac:Ta0169; -.
DR eggNOG; arCOG04237; Archaea.
DR HOGENOM; CLU_025068_2_1_2; -.
DR OMA; NEAVMHM; -.
DR OrthoDB; 39666at2157; -.
DR BRENDA; 2.3.3.16; 6324.
DR UniPathway; UPA00223; UER00717.
DR EvolutionaryTrace; P21553; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
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; IPR011278; 2-MeCitrate/Citrate_synth_II.
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; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01800; cit_synth_II; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Direct protein sequencing;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..385
FT /note="Citrate synthase"
FT /id="PRO_0000169978"
FT ACT_SITE 223
FT /evidence="ECO:0000305|PubMed:7704526"
FT ACT_SITE 263
FT /evidence="ECO:0000305|PubMed:7704526"
FT ACT_SITE 318
FT /evidence="ECO:0000305|PubMed:7704526"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2IFC"
FT STRAND 15..25
FT /evidence="ECO:0007829|PDB:2IFC"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:2IFC"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:2IFC"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 121..143
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:2IFC"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:2IFC"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 226..237
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:2IFC"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2IFC"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 288..308
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:2IFC"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 336..360
FT /evidence="ECO:0007829|PDB:2IFC"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:2IFC"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:2IFC"
SQ SEQUENCE 385 AA; 43072 MW; 9B7C2C88CEBCB690 CRC64;
MPETEEISKG LEDVNIKWTR LTTIDGNKGI LRYGGYSVED IIASGAQDEE IQYLFLYGNL
PTEQELRKYK ETVQKGYKIP DFVINAIRQL PRESDAVAMQ MAAVAAMAAS ETKFKWNKDT
DRDVAAEMIG RMSAITVNVY RHIMNMPAEL PKPSDSYAES FLNAAFGRKA TKEEIDAMNT
ALILYTDHEV PASTTAGLVA VSTLSDMYSG ITAALAALKG PLHGGAAEAA IAQFDEIKDP
AMVEKWFNDN IINGKKRLMG FGHRVYKTYD PRAKIFKGIA EKLSSKKPEV HKVYEIATKL
EDFGIKAFGS KGIYPNTDYF SGIVYMSIGF PLRNNIYTAL FALSRVTGWQ AHFIEYVEEQ
QRLIRPRAVY VGPAERKYVP IAERK
