CISY_CHICK
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 03-AUG-2022, entry version 127.
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 Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC 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: 1.9-
RT A structure of the ternary complex with oxaloacetate and carboxymethyl
RT 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 chicken
RT heart at 2.8-A resolution.";
RL Biochemistry 30:6031-6036(1991).
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=2.3.3.1; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10117, ECO:0000269|PubMed:2337600};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homodimer.
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}.
CC -!- CAUTION: This is an X-ray determined sequence which was established
CC using the sequence of pig citrate synthase and modifying it based on
CC the observed electron density. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 1AL6; X-ray; 1.85 A; A=1-80, A=82-433.
DR PDB; 1AMZ; X-ray; 1.80 A; A=3-80, A=82-433.
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=1-80, A/B=82-433.
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 SMR; P23007; -.
DR VEuPathDB; HostDB:geneid_100858903; -.
DR InParanoid; P23007; -.
DR OrthoDB; 1131452at2759; -.
DR PhylomeDB; P23007; -.
DR BRENDA; 2.3.3.1; 1306.
DR Reactome; R-GGA-372987; The tricarboxylic acid cycle.
DR SABIO-RK; P23007; -.
DR UniPathway; UPA00223; UER00717.
DR EvolutionaryTrace; P23007; -.
DR Proteomes; UP000000539; Unplaced.
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:0036440; F:citrate synthase activity; IDA:AgBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Transferase;
KW Tricarboxylic acid cycle.
FT CHAIN 1..433
FT /note="Citrate synthase, mitochondrial"
FT /id="PRO_0000169983"
FT ACT_SITE 274
FT ACT_SITE 320
FT ACT_SITE 375
FT HELIX 6..28
FT /evidence="ECO:0007829|PDB:1CSH"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:6CSC"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:1CSH"
FT TURN 43..47
FT /evidence="ECO:0007829|PDB:1CSH"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6CSC"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1CSH"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1CSH"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:1CSH"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6CSC"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 167..194
FT /evidence="ECO:0007829|PDB:1CSH"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:5CSC"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:1CSH"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1CSR"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:1CSH"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:1CSH"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 277..291
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 345..364
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 375..384
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:1CSH"
FT HELIX 393..414
FT /evidence="ECO:0007829|PDB:1CSH"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6CSC"
FT HELIX 427..433
FT /evidence="ECO:0007829|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
