CISY_PSEAE
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 03-AUG-2022, entry version 135.
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; Proteobacteria; 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 / 1C /
RC 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}.
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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; 287.DR97_309; -.
DR PaxDb; P14165; -.
DR PRIDE; P14165; -.
DR EnsemblBacteria; AAG04969; AAG04969; 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 OMA; TVGWCAQ; -.
DR PhylomeDB; P14165; -.
DR BioCyc; PAER208964:G1FZ6-1610-MON; -.
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; 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; IPR024176; Citrate_synthase_bac-typ.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR InterPro; IPR010953; Citrate_synthase_typ-I.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01798; cit_synth_I; 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
