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Database: UniProt
Entry: A0A0P0SBF9_9PSEU
LinkDB: A0A0P0SBF9_9PSEU
Original site: A0A0P0SBF9_9PSEU 
ID   A0A0P0SBF9_9PSEU        Unreviewed;       382 AA.
AC   A0A0P0SBF9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=citrate synthase (unknown stereospecificity) {ECO:0000256|ARBA:ARBA00012972};
DE            EC=2.3.3.16 {ECO:0000256|ARBA:ARBA00012972};
GN   ORFNames=AD017_10520 {ECO:0000313|EMBL:ALL81526.1};
OS   Pseudonocardia sp. EC080619-01.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL81526.1, ECO:0000313|Proteomes:UP000066228};
RN   [1] {ECO:0000313|EMBL:ALL81526.1, ECO:0000313|Proteomes:UP000066228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL81526.1,
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   -!- 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|RuleBase:RU003406}.
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DR   EMBL; CP012184; ALL81526.1; -; Genomic_DNA.
DR   RefSeq; WP_060574102.1; NZ_CP012184.1.
DR   AlphaFoldDB; A0A0P0SBF9; -.
DR   STRING; 1096856.AD017_10520; -.
DR   KEGG; pecq:AD017_10520; -.
DR   PATRIC; fig|1096856.3.peg.2214; -.
DR   OrthoDB; 9800864at2; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000066228; Chromosome.
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; 2.
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; IPR036969; Citrate_synthase_sf.
DR   PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR11739:SF23; CITRATE SYNTHASE 2-RELATED; 1.
DR   Pfam; PF00285; Citrate_synt; 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:ALL81526.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066228};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003406}.
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  41321 MW;  0BD8C46BEDBBCCA3 CRC64;
     MTETATSPTH EVPPPPPGFR SGLEGHVAFR TEIAEPDKDG GALRYRGVDL EDLAGKVTFG
     DVWALLVDGR FGQGLPPAEP FPIPVHTGDV RVDVQAALAM LAPYWGYRPL LDIDKAEARD
     NLARASVMAL SYVAQSARGI GVAAVPQSRI DECSTITERF MTRWRGEPDP RHVAAVDAYW
     VSAAEHGMNA STFTARVIAS TGADAAASLS GAIGAMSGPL HGGAPARVLP MIDEVERTGD
     AESLVTGMLD RKEKLMGFGH RVYRAEDPRA RVLRRTCQEL GAPRFEVAAE LERTALSVLR
     ERRPDRPIET NVEFWAAVVL DFAEVPPHMM PAMFTSARTA GWSAHVLEQK REGKLVRPSA
     QYIGPGPRSP EQVDGWDAVT GS
//
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