ID CISY_CHICK Reviewed; 433 AA.
AC P23007;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 01-MAY-2013, entry version 91.
DE RecName: Full=Citrate synthase, mitochondrial;
DE EC=2.3.3.1;
GN Name=CS;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RC TISSUE=Heart muscle;
RX PubMed=2337600; DOI=10.1021/bi00461a002;
RA Karpusas M., Branchaud B., Remington S.J.;
RT "Proposed mechanism for the condensation reaction of citrate synthase:
RT 1.9-A structure of the ternary complex with oxaloacetate and
RT carboxymethyl coenzyme A.";
RL Biochemistry 29:2213-2219(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF OPEN CONFORMATION.
RX PubMed=2043641; DOI=10.1021/bi00238a029;
RA Liao D.-I., Karpusas M., Remington S.J.;
RT "Crystal structure of an open conformation of citrate synthase from
RT chicken heart at 2.8-A resolution.";
RL Biochemistry 30:6031-6036(1991).
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate +
CC CoA.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC isocitrate from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells
CC capable of oxidative metabolism.
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC -!- CAUTION: This is an X-ray determined sequence which was
CC established using the sequence of pig citrate synthase and
CC modifying it based on the observed electron density.
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DR IPI; IPI00574841; -.
DR PDB; 1AL6; X-ray; 1.85 A; A=1-427.
DR PDB; 1AMZ; X-ray; 1.80 A; A=3-427.
DR PDB; 1CSC; X-ray; 1.70 A; A=1-433.
DR PDB; 1CSH; X-ray; 1.65 A; A=3-430.
DR PDB; 1CSI; X-ray; 1.70 A; A=3-430.
DR PDB; 1CSR; X-ray; 1.70 A; A=3-430.
DR PDB; 1CSS; X-ray; 1.70 A; A=3-430.
DR PDB; 2CSC; X-ray; 1.70 A; A=1-433.
DR PDB; 3CSC; X-ray; 1.90 A; A=1-433.
DR PDB; 4CSC; X-ray; 1.90 A; A=1-433.
DR PDB; 5CSC; X-ray; 2.80 A; A/B=1-433.
DR PDB; 5CTS; X-ray; 1.90 A; A=1-433.
DR PDB; 6CSC; X-ray; 2.25 A; A/B=1-427.
DR PDB; 6CTS; X-ray; 2.50 A; A=1-433.
DR PDBsum; 1AL6; -.
DR PDBsum; 1AMZ; -.
DR PDBsum; 1CSC; -.
DR PDBsum; 1CSH; -.
DR PDBsum; 1CSI; -.
DR PDBsum; 1CSR; -.
DR PDBsum; 1CSS; -.
DR PDBsum; 2CSC; -.
DR PDBsum; 3CSC; -.
DR PDBsum; 4CSC; -.
DR PDBsum; 5CSC; -.
DR PDBsum; 5CTS; -.
DR PDBsum; 6CSC; -.
DR PDBsum; 6CTS; -.
DR PRIDE; P23007; -.
DR HOVERGEN; HBG005336; -.
DR Reactome; REACT_115655; Metabolism.
DR UniPathway; UPA00223; UER00717.
DR EvolutionaryTrace; P23007; -.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; ISS:AgBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome.
DR Gene3D; 1.10.580.10; -; 1.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR002020; Citrate_synthase-like.
DR InterPro; IPR016141; Citrate_synthase-like_core.
DR InterPro; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR010109; Citrate_synthase_euk.
DR PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; Citrate_synthase_core; 1.
DR TIGRFAMs; TIGR01793; cit_synth_euk; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Mitochondrion; Reference proteome;
KW Transferase; Tricarboxylic acid cycle.
FT CHAIN 1 433 Citrate synthase, mitochondrial.
FT /FTId=PRO_0000169983.
FT ACT_SITE 274 274
FT ACT_SITE 320 320
FT ACT_SITE 375 375
FT HELIX 6 28
FT STRAND 31 34
FT HELIX 38 42
FT TURN 43 47
FT STRAND 49 52
FT STRAND 55 59
FT TURN 60 62
FT STRAND 63 66
FT HELIX 71 77
FT STRAND 85 87
FT HELIX 89 98
FT HELIX 104 117
FT HELIX 122 130
FT HELIX 137 147
FT HELIX 148 151
FT HELIX 153 159
FT HELIX 164 166
FT HELIX 167 194
FT TURN 195 197
FT HELIX 209 217
FT HELIX 222 234
FT STRAND 240 242
FT HELIX 243 252
FT TURN 253 255
FT HELIX 258 269
FT TURN 272 276
FT HELIX 277 291
FT HELIX 298 310
FT HELIX 328 340
FT HELIX 345 364
FT HELIX 375 384
FT HELIX 390 392
FT HELIX 393 414
FT STRAND 423 425
FT HELIX 427 430
SQ SEQUENCE 433 AA; 47378 MW; 6942294BA95A9E06 CRC64;
ASSTNLKDVL AALIPKEQAR IKTFRQQHGG TALGQITVDM SYGGMRGMKG LVYETSVLDP
DEGIRFRGFS IPECQKLLPK GGXGGEPLPE GLFWLLVTGQ IPTGAQVSWL SKEWAKRAAL
PSHVVTMLDN FPTNLHPMSQ LSAAITALNS ESNFARAYAE GILRTKYWEM VYESAMDLIA
KLPCVAAKIY RNLYRAGSSI GAIDSKLDWS HNFTNMLGYT DAQFTELMRL YLTIHSDHEG
GNVSAHTSHL VGSALSDPYL SFAAAMNGLA GPLHGLANQE VLGWLAQLQK AXXXAGADAS
LRDYIWNTLN SGRVVPGYGH AVLRKTDPRY TCQREFALKH LPGDPMFKLV AQLYKIVPNV
LLEQGAAANP WPNVDAHSGV LLQYYGMTEM NYYTVLFGVS RALGVLAQLI WSRALGFPLE
RPKSMSTDGL IAL
//