CISY_PYRFU
ID CISY_PYRFU Reviewed; 377 AA.
AC Q53554;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Citrate synthase;
DE EC=2.3.3.16;
GN Name=gltA; OrderedLocusNames=PF0203;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8532683; DOI=10.1093/protein/8.6.583;
RA Muir J.M., Russell R.J., Hough D.W., Danson M.J.;
RT "Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus
RT furiosus.";
RL Protein Eng. 8:583-592(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9254593; DOI=10.1021/bi9705321;
RA Russell R.J., Ferguson J.M., Hough D.W., Danson M.J., Taylor G.L.;
RT "The crystal structure of citrate synthase from the hyperthermophilic
RT archaeon Pyrococcus furiosus at 1.9-A resolution.";
RL Biochemistry 36:9983-9994(1997).
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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; S81109; AAB35835.2; -; Genomic_DNA.
DR EMBL; AE009950; AAL80327.1; -; Genomic_DNA.
DR RefSeq; WP_011011316.1; NC_018092.1.
DR PDB; 1AJ8; X-ray; 1.90 A; A/B=7-377.
DR PDBsum; 1AJ8; -.
DR AlphaFoldDB; Q53554; -.
DR SMR; Q53554; -.
DR STRING; 186497.PF0203; -.
DR EnsemblBacteria; AAL80327; AAL80327; PF0203.
DR GeneID; 41711994; -.
DR KEGG; pfu:PF0203; -.
DR PATRIC; fig|186497.12.peg.211; -.
DR eggNOG; arCOG04237; Archaea.
DR HOGENOM; CLU_025068_2_1_2; -.
DR OMA; TVGWCAQ; -.
DR OrthoDB; 39666at2157; -.
DR PhylomeDB; Q53554; -.
DR BRENDA; 2.3.3.1; 5243.
DR BRENDA; 2.3.3.16; 5243.
DR UniPathway; UPA00223; UER00717.
DR EvolutionaryTrace; Q53554; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
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 PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01800; cit_synth_II; 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 CHAIN 2..377
FT /note="Citrate synthase"
FT /id="PRO_0000169976"
FT ACT_SITE 263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1AJ8"
FT STRAND 15..25
FT /evidence="ECO:0007829|PDB:1AJ8"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:1AJ8"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 95..109
FT /evidence="ECO:0007829|PDB:1AJ8"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 119..144
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:1AJ8"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:1AJ8"
FT TURN 222..226
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 286..302
FT /evidence="ECO:0007829|PDB:1AJ8"
FT TURN 303..307
FT /evidence="ECO:0007829|PDB:1AJ8"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 316..321
FT /evidence="ECO:0007829|PDB:1AJ8"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 330..350
FT /evidence="ECO:0007829|PDB:1AJ8"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:1AJ8"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:1AJ8"
SQ SEQUENCE 377 AA; 43050 MW; A73E70EF123BE44B CRC64;
MNTEKYLAKG LEDVYIDQTN ICYIDGKEGK LYYRGYSVEE LAELSTFEEV VYLLWWGKLP
SLSELENFKK ELAKSRGLPK EVIEIMEALP KNTHPMGALR TIISYLGNID DSGDIPVTPE
EVYRIGISVT AKIPTIVANW YRIKNGLEYV PPKEKLSHAA NFLYMLHGEE PPKEWEKAMD
VALILYAEHE INASTLAVMT VGSTLSDYYS AILAGIGALK GPIHGGAVEE AIKQFMEIGS
PEKVEEWFFK ALQQKRKIMG AGHRVYKTYD PRARIFKKYA SKLGDKKLFE IAERLERLVE
EYLSKKGISI NVDYWSGLVF YGMKIPIELY TTIFAMGRIA GWTAHLAEYV SHNRIIRPRL
QYVGEIGKKY LPIELRR
