CISY_STRHY
ID CISY_STRHY Reviewed; 20 AA.
AC P20903;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Citrate synthase;
DE EC=2.3.3.16;
DE Flags: Fragment;
GN Name=gltA;
OS Streptomyces hygroscopicus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=1912;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 21705 / DSM 41527 / SF-1293;
RX PubMed=1368511; DOI=10.1271/bbb1961.54.463;
RA Shimotohno K.W., Imai S., Murakami T., Seto H.;
RT "Purification and characterization of citrate synthase from Streptomyces
RT hygroscopicus SF-1293 and comparison of its properties with those of 2-
RT phosphinomethylmalic acid synthase.";
RL Agric. Biol. Chem. 54:463-470(1990).
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: Homohexamer.
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 ---------------------------------------------------------------------------
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 PIR; PQ0046; PQ0046.
DR AlphaFoldDB; P20903; -.
DR STRING; 68042.GCA_001553435_06284; -.
DR UniPathway; UPA00223; UER00717.
DR GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Direct protein sequencing; Transferase;
KW Tricarboxylic acid cycle.
FT CHAIN 1..>20
FT /note="Citrate synthase"
FT /id="PRO_0000169972"
FT NON_TER 20
SQ SEQUENCE 20 AA; 2234 MW; C527EC7A87119597 CRC64;
SDNSVVLRYG DGEYSYPVVD