ID A0A0P0SDN6_9PSEU Unreviewed; 374 AA.
AC A0A0P0SDN6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369};
GN ORFNames=AD017_16000 {ECO:0000313|EMBL:ALL82305.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL82305.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL82305.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL82305.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
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; CP012184; ALL82305.1; -; Genomic_DNA.
DR RefSeq; WP_060574714.1; NZ_CP012184.1.
DR AlphaFoldDB; A0A0P0SDN6; -.
DR STRING; 1096856.AD017_16000; -.
DR KEGG; pecq:AD017_16000; -.
DR PATRIC; fig|1096856.3.peg.3359; -.
DR OrthoDB; 9800864at2; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000066228; 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:ALL82305.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000066228};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001369}.
FT ACT_SITE 262
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
FT ACT_SITE 313
FT /evidence="ECO:0000256|PIRSR:PIRSR001369-1"
SQ SEQUENCE 374 AA; 40975 MW; CF5961B051461A07 CRC64;
MTGDPGIRRG LVGVVADSTA ISDVDPGHNV LLYRGYPAQD LVERHGFLEV AHLLWTGELP
DSGELVELDG RERSLRTIEP ALERLLLSLP PACHPMDVLR TAVSWLGAVD PEADDPSPEA
GREKAMRLLA VLPTVVALEQ RRRRGQEPIA PREDLPYAEN FFHMTFGQVP EPEVVRAFEV
SMMLFAEHSF NASAFTARVV TSTRSDLHSA VVGAIGALKG SLHGGANQAV MEQFAEIGDP
DDVDEWLNAR LGAGDTVMGF GHRVYKRGDS RVPILHRELR RIADLRGGRD LLAFYEVLAG
AMLRDKGLRP NLDYAAGPLY HLMGFDTPLF TPLFVMSRIS GWAAHVVEQA GDNVLIRPVA
AYDGKARREV PAGR
//
