ID A1AXW0_RUTMC Unreviewed; 378 AA.
AC A1AXW0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369};
GN OrderedLocusNames=Rmag_1063 {ECO:0000313|EMBL:ABL02767.1};
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthturnera.
OX NCBI_TaxID=413404 {ECO:0000313|EMBL:ABL02767.1, ECO:0000313|Proteomes:UP000002587};
RN [1] {ECO:0000313|EMBL:ABL02767.1, ECO:0000313|Proteomes:UP000002587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm {ECO:0000313|EMBL:ABL02767.1};
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
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|ARBA:ARBA00000308};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2. {ECO:0000256|ARBA:ARBA00004751}.
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|PIRNR:PIRNR001369}.
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DR EMBL; CP000488; ABL02767.1; -; Genomic_DNA.
DR RefSeq; WP_011738392.1; NC_008610.1.
DR AlphaFoldDB; A1AXW0; -.
DR STRING; 413404.Rmag_1063; -.
DR KEGG; rma:Rmag_1063; -.
DR eggNOG; COG0372; Bacteria.
DR HOGENOM; CLU_025068_2_1_6; -.
DR OrthoDB; 9800864at2; -.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000002587; Chromosome.
DR GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd06112; citrate_synt_like_1_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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:ABL02767.1};
KW Transferase {ECO:0000256|PIRNR:PIRNR001369, ECO:0000313|EMBL:ABL02767.1}.
FT ACT_SITE 261
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 317
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 378 AA; 42330 MW; F2800DBCA5FFA15D CRC64;
MIEYIPGLAG VPATESSISY IDGKNGILTY RGYSIEDLVK YGSFEEVSML LRDGELPDKN
KLDNFKNILH KRYEVKRNIR SMMWSLPANG HPMNVLQTTI AAMATFYPDA GAQNPDSVYT
QGALTKIISN MSTLVAMWAR ISAGYDPIPP SRGMSYAKNF LYMSFGEEPD DDIVKLFDAC
LILHAEHTIN ASTFSAMVTA STLANPFASI SAAVGTLAGS LHGGANEDVL KMLDEIGDAK
NARAYIKNRL KNKQIIWGMG HREYSVKDPR ASILQSMIED YVKKSNMHFS KRFETALEVE
RICEDLLSSK GVYPNVDFYS GILYAEIFKI PQTHFTPIFA MARSAGWTAH WHEQVGHNRI
FRPAQIYIGS NFRNYSKK
//