P23007 (CISY_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Citrate synthase, mitochondrial
EC=2.3.3.1

Gene names

Name:

CS

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion matrix.
Miscellaneous	Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Sequence similarities	Belongs to the citrate synthase family.
Caution	This is an X-ray determined sequence which was established using the sequence of pig citrate synthase and modifying it based on the observed electron density.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	citrate (Si)-synthase activity Inferred from sequence or structural similarity. Source: AgBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 433

433

Citrate synthase, mitochondrial

PRO_0000169983

Sites

Active site

274

1

Active site

320

1

Active site

375

1

Secondary structure

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433

Helix Strand Turn

Details...

Helix

6 – 28

23

Beta strand

32 – 37

6

Helix

38 – 42

5

Turn

43 – 47

5

Beta strand

49 – 52

4

Beta strand

55 – 59

5

Turn

60 – 62

3

Beta strand

63 – 66

4

Helix

71 – 77

7

Helix

89 – 98

10

Helix

104 – 117

14

Helix

122 – 130

9

Helix

137 – 147

11

Helix

148 – 151

4

Helix

153 – 160

8

Helix

164 – 166

3

Helix

167 – 194

28

Helix

209 – 217

9

Helix

222 – 234

13

Beta strand

240 – 242

3

Helix

243 – 252

10

Turn

253 – 255

3

Helix

258 – 269

12

Turn

272 – 276

5

Helix

277 – 292

16

Helix

298 – 310

13

Helix

328 – 340

13

Helix

345 – 364

20

Helix

375 – 384

10

Helix

390 – 392

3

Helix

393 – 414

22

Beta strand

423 – 425

3

Helix

427 – 430

4

Sequences

	Sequence		Length	Mass (Da)
	P23007 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 6942294BA95A9E06	FASTA	433	47,378
	10 20 30 40 50 60 ASSTNLKDVL AALIPKEQAR IKTFRQQHGG TALGQITVDM SYGGMRGMKG LVYETSVLDP 70 80 90 100 110 120 DEGIRFRGFS IPECQKLLPK GGXGGEPLPE GLFWLLVTGQ IPTGAQVSWL SKEWAKRAAL 130 140 150 160 170 180 PSHVVTMLDN FPTNLHPMSQ LSAAITALNS ESNFARAYAE GILRTKYWEM VYESAMDLIA 190 200 210 220 230 240 KLPCVAAKIY RNLYRAGSSI GAIDSKLDWS HNFTNMLGYT DAQFTELMRL YLTIHSDHEG 250 260 270 280 290 300 GNVSAHTSHL VGSALSDPYL SFAAAMNGLA GPLHGLANQE VLGWLAQLQK AXXXAGADAS 310 320 330 340 350 360 LRDYIWNTLN SGRVVPGYGH AVLRKTDPRY TCQREFALKH LPGDPMFKLV AQLYKIVPNV 370 380 390 400 410 420 LLEQGAAANP WPNVDAHSGV LLQYYGMTEM NYYTVLFGVS RALGVLAQLI WSRALGFPLE 430 RPKSMSTDGL IAL

References

[1]	"Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A." Karpusas M., Branchaud B., Remington S.J. Biochemistry 29:2213-2219(1990) [PubMed: 2337600] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). Tissue: Heart muscle.
[2]	"Crystal structure of an open conformation of citrate synthase from chicken heart at 2.8-A resolution." Liao D.-I., Karpusas M., Remington S.J. Biochemistry 30:6031-6036(1991) [PubMed: 2043641] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF OPEN CONFORMATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

IPI

IPI00574841.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AL6	X-ray	1.85	A	1-427	[»]
1AMZ	X-ray	1.80	A	3-427	[»]
1CSC	X-ray	1.70	A	1-433	[»]
1CSH	X-ray	1.65	A	3-430	[»]
1CSI	X-ray	1.70	A	3-430	[»]
1CSR	X-ray	1.70	A	3-430	[»]
1CSS	X-ray	1.70	A	3-430	[»]
2CSC	X-ray	1.70	A	1-433	[»]
3CSC	X-ray	1.90	A	1-433	[»]
4CSC	X-ray	1.90	A	1-433	[»]
5CSC	X-ray	2.80	A/B	1-433	[»]
5CTS	X-ray	1.90	A	1-433	[»]
6CSC	X-ray	2.25	A/B	1-427	[»]
6CTS	X-ray	2.50	A	1-433	[»]

ModBase

Search...

Proteomic databases

PRIDE

P23007.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG005336.

PhylomeDB

P23007.

Family and domain databases

InterPro

IPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR010109. Citrate_synthase_euk.
[Graphical view]

Gene3D

G3DSA:1.10.580.10. Citrate_synthase_lrg_a-sub. 1 hit.

PANTHER

PTHR11739. Citrate_synth. 1 hit.

Pfam

PF00285. Citrate_synt. 1 hit.
[Graphical view]

PRINTS

PR00143. CITRTSNTHASE.

SUPFAM

SSF48256. Citrate_synthase_core. 1 hit.

TIGRFAMs

TIGR01793. Cit_synth_euk. 1 hit.

PROSITE

PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CISY_CHICK

Accession

Primary (citable) accession number: P23007

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	September 21, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program