ID CISY_PSEAE Reviewed; 428 AA. AC P14165; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 142. DE RecName: Full=Citrate synthase {ECO:0000303|PubMed:2507528}; DE EC=2.3.3.16 {ECO:0000269|PubMed:2507528}; GN Name=gltA; OrderedLocusNames=PA1580; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-9, CATALYTIC RP ACTIVITY, AND ACTIVITY REGULATION. RC STRAIN=ATCC 7700 / UM74; RX PubMed=2507528; DOI=10.1128/jb.171.10.5542-5550.1989; RA Donald L.J., Molgat G.F., Duckworth H.W.; RT "Cloning, sequencing, and expression of the gene for NADH-sensitive citrate RT synthase of Pseudomonas aeruginosa."; RL J. Bacteriol. 171:5542-5550(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). 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; CC Evidence={ECO:0000269|PubMed:2507528}; CC -!- ACTIVITY REGULATION: Allosterically inhibited by NADH. CC {ECO:0000269|PubMed:2507528}. 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 EMBL; M29728; AAA25769.1; -; Genomic_DNA. DR EMBL; AE004091; AAG04969.1; -; Genomic_DNA. DR PIR; A33596; YKPSCA. DR PIR; B83448; B83448. DR RefSeq; NP_250271.1; NC_002516.2. DR RefSeq; WP_003087400.1; NZ_QZGE01000003.1. DR PDB; 6ZU0; X-ray; 3.40 A; A/B/C/D/E/F=1-428. DR PDBsum; 6ZU0; -. DR AlphaFoldDB; P14165; -. DR SMR; P14165; -. DR STRING; 208964.PA1580; -. DR PaxDb; 208964-PA1580; -. DR GeneID; 882117; -. DR KEGG; pae:PA1580; -. DR PATRIC; fig|208964.12.peg.1639; -. DR PseudoCAP; PA1580; -. DR HOGENOM; CLU_025068_0_0_6; -. DR InParanoid; P14165; -. DR OrthoDB; 9800864at2; -. DR PhylomeDB; P14165; -. DR BioCyc; PAER208964:G1FZ6-1610-MONOMER; -. DR UniPathway; UPA00223; UER00717. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IDA:PseudoCAP. DR GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:InterPro. DR GO; GO:0036440; F:citrate synthase activity; IDA:PseudoCAP. DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:PseudoCAP. DR CDD; cd06114; EcCS_like; 1. DR Gene3D; 2.20.28.60; -; 1. DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1. DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 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; IPR024176; Citrate_synthase_bac-typ. DR InterPro; IPR036969; Citrate_synthase_sf. DR InterPro; IPR010953; Citrate_synthase_typ-I. DR NCBIfam; TIGR01798; cit_synth_I; 1. DR PANTHER; PTHR42871; CITRATE SYNTHASE; 1. DR PANTHER; PTHR42871:SF1; CITRATE SYNTHASE; 1. DR Pfam; PF00285; Citrate_synt; 1. DR PIRSF; PIRSF001369; Citrate_synth; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR SUPFAM; SSF48256; Citrate synthase; 1. DR PROSITE; PS00480; CITRATE_SYNTHASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Direct protein sequencing; KW Reference proteome; Transferase; Tricarboxylic acid cycle. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2507528" FT CHAIN 2..428 FT /note="Citrate synthase" FT /id="PRO_0000169952" FT ACT_SITE 265 FT /evidence="ECO:0000250|UniProtKB:P21553" FT ACT_SITE 306 FT /evidence="ECO:0000250|UniProtKB:P21553" FT ACT_SITE 363 FT /evidence="ECO:0000250|UniProtKB:P21553" FT CONFLICT 153 FT /note="N -> T (in Ref. 1; AAA25769)" FT /evidence="ECO:0000305" FT CONFLICT 159 FT /note="E -> Q (in Ref. 1; AAA25769)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 16..21 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 28..31 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:6ZU0" FT TURN 62..65 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 74..79 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 83..92 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 98..110 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 117..122 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 131..145 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 155..181 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 194..203 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 214..225 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 234..243 FT /evidence="ECO:0007829|PDB:6ZU0" FT TURN 244..246 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 249..261 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 263..266 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 268..279 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 285..293 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 302..305 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 307..311 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 316..330 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 335..349 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 351..355 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 362..372 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 377..379 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 380..401 FT /evidence="ECO:0007829|PDB:6ZU0" FT STRAND 410..413 FT /evidence="ECO:0007829|PDB:6ZU0" FT HELIX 424..426 FT /evidence="ECO:0007829|PDB:6ZU0" SQ SEQUENCE 428 AA; 47695 MW; 3E1875ED70266C37 CRC64; MADKKAQLII EGSAPVELPV LSGTMGPDVV DVRGLTATGH FTFDPGFMST ASCESKITYI DGDKGVLLHR GYPIEQLAEK SDYLETCYLL LNGELPTAAQ KEQFVGTIKN HTMVHEQLKT FFNGFRRDAH PMAVMCGVIG ALSAFYHDSL DINNPKHREV SAHRLIAKMP TIAAMVYKYS KGEPMMYPRN DLNYAENFLH MMFNTPCETK PISPVLAKAM DRIFILHADH EQNASTSTVR LAGSSGANPF ACIASGIAAL WGPAHGGANE AVLRMLDEIG DVSNIDKFVE KAKDKNDPFK LMGFGHRVYK NFDPRAKVMK QTCDEVLQEL GINDPQLELA MKLEEIARHD PYFVERNLYP NVDFYSGIIL KAIGIPTSMF TVIFALARTV GWISHWQEML SGPYKIGRPR QLYTGHTQRD FTALKDRG //