ID G0EGE5_PYRF1 Unreviewed; 383 AA.
AC G0EGE5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369, ECO:0000256|RuleBase:RU000441};
DE EC=2.3.3.16 {ECO:0000256|PIRNR:PIRNR001369};
GN OrderedLocusNames=Pyrfu_1311 {ECO:0000313|EMBL:AEM39170.1};
OS Pyrolobus fumarii (strain DSM 11204 / 1A).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrolobus.
OX NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM39170.1, ECO:0000313|Proteomes:UP000001037};
RN [1] {ECO:0000313|EMBL:AEM39170.1, ECO:0000313|Proteomes:UP000001037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX PubMed=21886865;
RA Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H.,
RA Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT Pyrolobus fumarii type strain (1A).";
RL Stand. Genomic Sci. 4:381-392(2011).
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:0000256|PIRNR:PIRNR001369};
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|PIRNR:PIRNR001369,
CC ECO:0000256|RuleBase:RU000441}.
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DR EMBL; CP002838; AEM39170.1; -; Genomic_DNA.
DR AlphaFoldDB; G0EGE5; -.
DR STRING; 694429.Pyrfu_1311; -.
DR KEGG; pfm:Pyrfu_1311; -.
DR eggNOG; arCOG04237; Archaea.
DR HOGENOM; CLU_025068_2_1_2; -.
DR InParanoid; G0EGE5; -.
DR Proteomes; UP000001037; Chromosome.
DR GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd06118; citrate_synt_like_1; 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 PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR PANTHER; PTHR11739:SF4; CITRATE SYNTHASE, PEROXISOMAL; 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 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AEM39170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001037};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001369}.
FT ACT_SITE 263
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 319
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 383 AA; 42575 MW; A5A0F07B2AB11C81 CRC64;
MRGLDGVYVA ETRISYVDGE KGRLWYRGYA VDELARKATF EEVAYLLIHG KLPNREELEE
FRSRLIAARR IPEHVIEVAE KLPQNLHVLD KMRVLVTLLY GWYGDGKPRM LTSKQVDAKP
VIEAGTGLVG AAPRLLGIIA ALEEGRELPS EKFELDSHAA YTLYALTGRE PSLPERDAFN
TLLILYADHE LPASTFAAMV AASTLTDIYS AIDAALATLK GPLHGGALEE VAKMLLEIGD
PENAEKYVEN VLSSGKRLMG FGHRVYKTYD PRSLILKKVA SIIANAVGGE ARRLYETAVA
VENAALKRLA RKNIYPNVDF WASVLLYALG IKPRYYTGVF AVARIVGWVA HVAEYVARNR
LIRPRALYTG PLNLPYLPLE ARQ
//
