ID A9WQB8_RENSM Unreviewed; 372 AA.
AC A9WQB8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369};
GN OrderedLocusNames=RSal33209_0824 {ECO:0000313|EMBL:ABY22568.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY22568.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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.
CC {ECO:0000256|ARBA:ARBA00005163}.
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|PIRNR:PIRNR001369,
CC ECO:0000256|RuleBase:RU003406}.
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DR EMBL; CP000910; ABY22568.1; -; Genomic_DNA.
DR RefSeq; WP_012244265.1; NC_010168.1.
DR AlphaFoldDB; A9WQB8; -.
DR SMR; A9WQB8; -.
DR STRING; 288705.RSal33209_0824; -.
DR KEGG; rsa:RSal33209_0824; -.
DR eggNOG; COG0372; Bacteria.
DR HOGENOM; CLU_025068_2_1_11; -.
DR OMA; NEAVMHM; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000002007; 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; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 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 NCBIfam; TIGR01800; cit_synth_II; 1.
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:ABY22568.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001369}.
FT ACT_SITE 264
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 315
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 372 AA; 40569 MW; CBFDF9499306A660 CRC64;
MADETQDIQK GLAGVVVDYT AVSKVNPGSN SLLYRGYPVQ ELSAKKSFEE VALLLWNGEL
PSEAELTTFE ALERANRALD GNVKAAIDLL PTSCHPMDVC RTATSVIGAN HALAEDSSPE
ANLQKAKELF AAMPAVVAYD QRRRHGLDPV EPREDLGYSA NFLWMTFGEE TAPEVVEAFN
VSMILYAEHS FNASTFTTRV ITSTLADLHS AVTGAIGALK GPLHGGANEA VMHTFEEIQS
TGVDAKTWLT DALAQKKKIM GFGHRVYKNG DSRVPTMKAA LEKMSAHYQR EDMLDLYSAL
ESAMGEAKNI KPNLDYPAGP TYHLMGFDTP TFTPLFVASR ITGWTAHIME QAASNSLIRP
LSAYNGVDER HL
//