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Database: UniProt
Entry: P23007
LinkDB: P23007
Original site: P23007 
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   26-NOV-2014, entry version 103.
DE   RecName: Full=Citrate synthase, mitochondrial;
DE            EC=2.3.3.1;
DE   AltName: Full=Citrate (Si)-synthase;
GN   Name=CS;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND CATALYTIC ACTIVITY.
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. {ECO:0000255|PROSITE-ProRule:PRU10117,
CC       ECO:0000269|PubMed:2337600}.
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. {ECO:0000305}.
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.
CC       {ECO:0000305}.
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DR   PDB; 1AL6; X-ray; 1.85 A; A=1-433.
DR   PDB; 1AMZ; X-ray; 1.80 A; A=3-433.
DR   PDB; 1CSC; X-ray; 1.70 A; A=1-433.
DR   PDB; 1CSH; X-ray; 1.65 A; A=3-433.
DR   PDB; 1CSI; X-ray; 1.70 A; A=3-433.
DR   PDB; 1CSR; X-ray; 1.70 A; A=3-433.
DR   PDB; 1CSS; X-ray; 1.70 A; A=3-433.
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=1-433.
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   InParanoid; P23007; -.
DR   PhylomeDB; P23007; -.
DR   Reactome; REACT_115536; The tricarboxylic acid cycle.
DR   UniPathway; UPA00223; UER00717.
DR   EvolutionaryTrace; P23007; -.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:AgBase.
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; SSF48256; 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       {ECO:0000244|PDB:1CSH}.
FT   STRAND       31     34       {ECO:0000244|PDB:6CSC}.
FT   HELIX        38     42       {ECO:0000244|PDB:1CSH}.
FT   TURN         43     47       {ECO:0000244|PDB:1CSH}.
FT   STRAND       49     52       {ECO:0000244|PDB:6CSC}.
FT   STRAND       55     59       {ECO:0000244|PDB:1CSH}.
FT   TURN         60     62       {ECO:0000244|PDB:1CSH}.
FT   STRAND       63     66       {ECO:0000244|PDB:1CSH}.
FT   HELIX        71     77       {ECO:0000244|PDB:1CSH}.
FT   STRAND       85     87       {ECO:0000244|PDB:6CSC}.
FT   HELIX        89     98       {ECO:0000244|PDB:1CSH}.
FT   HELIX       104    117       {ECO:0000244|PDB:1CSH}.
FT   HELIX       122    130       {ECO:0000244|PDB:1CSH}.
FT   HELIX       137    147       {ECO:0000244|PDB:1CSH}.
FT   HELIX       148    151       {ECO:0000244|PDB:1CSH}.
FT   HELIX       153    159       {ECO:0000244|PDB:1CSH}.
FT   HELIX       164    166       {ECO:0000244|PDB:1CSH}.
FT   HELIX       167    194       {ECO:0000244|PDB:1CSH}.
FT   TURN        195    197       {ECO:0000244|PDB:5CSC}.
FT   HELIX       209    217       {ECO:0000244|PDB:1CSH}.
FT   HELIX       222    234       {ECO:0000244|PDB:1CSH}.
FT   STRAND      240    242       {ECO:0000244|PDB:1CSR}.
FT   HELIX       243    252       {ECO:0000244|PDB:1CSH}.
FT   TURN        253    255       {ECO:0000244|PDB:1CSH}.
FT   HELIX       258    269       {ECO:0000244|PDB:1CSH}.
FT   TURN        272    276       {ECO:0000244|PDB:1CSH}.
FT   HELIX       277    291       {ECO:0000244|PDB:1CSH}.
FT   HELIX       298    310       {ECO:0000244|PDB:1CSH}.
FT   HELIX       328    340       {ECO:0000244|PDB:1CSH}.
FT   HELIX       345    364       {ECO:0000244|PDB:1CSH}.
FT   HELIX       375    384       {ECO:0000244|PDB:1CSH}.
FT   HELIX       390    392       {ECO:0000244|PDB:1CSH}.
FT   HELIX       393    414       {ECO:0000244|PDB:1CSH}.
FT   STRAND      423    425       {ECO:0000244|PDB:6CSC}.
FT   HELIX       427    433       {ECO:0000244|PDB:1CSH}.
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
//
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