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Database: UniProt
Entry: A0A3P1W290_9FUSO
LinkDB: A0A3P1W290_9FUSO
Original site: A0A3P1W290_9FUSO 
ID   A0A3P1W290_9FUSO        Unreviewed;       430 AA.
AC   A0A3P1W290;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Citrate lyase holo-[acyl-carrier protein] synthase {ECO:0000313|EMBL:RRD40692.1};
DE            EC=2.7.7.61 {ECO:0000313|EMBL:RRD40692.1};
GN   Name=citX {ECO:0000313|EMBL:RRD40692.1};
GN   ORFNames=EII29_01810 {ECO:0000313|EMBL:RRD40692.1};
OS   Leptotrichia sp. OH3620_COT-345.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=2491048 {ECO:0000313|EMBL:RRD40692.1, ECO:0000313|Proteomes:UP000280115};
RN   [1] {ECO:0000313|EMBL:RRD40692.1, ECO:0000313|Proteomes:UP000280115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH3620_COT-345 {ECO:0000313|EMBL:RRD40692.1,
RC   ECO:0000313|Proteomes:UP000280115};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + apo-
CC         [citrate lyase ACP] = diphosphate + holo-[citrate lyase ACP];
CC         Xref=Rhea:RHEA:16333, Rhea:RHEA-COMP:10157, Rhea:RHEA-COMP:10158,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:61378,
CC         ChEBI:CHEBI:82683; EC=2.7.7.61;
CC         Evidence={ECO:0000256|ARBA:ARBA00000145};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-
CC         3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57328, ChEBI:CHEBI:61378; EC=2.4.2.52;
CC         Evidence={ECO:0000256|ARBA:ARBA00001210};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RRD40692.1}.
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DR   EMBL; RQYW01000002; RRD40692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P1W290; -.
DR   OrthoDB; 114886at2; -.
DR   Proteomes; UP000280115; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0050519; F:holo-citrate lyase synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   GO; GO:0051191; P:prosthetic group biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.4200.10; Triphosphoribosyl-dephospho-CoA protein; 1.
DR   InterPro; IPR002736; CitG.
DR   InterPro; IPR005551; CitX.
DR   NCBIfam; TIGR03124; citrate_citX; 1.
DR   PANTHER; PTHR30201:SF2; 2-(5''-TRIPHOSPHORIBOSYL)-3'-DEPHOSPHOCOENZYME-A SYNTHASE; 1.
DR   PANTHER; PTHR30201; TRIPHOSPHORIBOSYL-DEPHOSPHO-COA SYNTHASE; 1.
DR   Pfam; PF01874; CitG; 1.
DR   Pfam; PF03802; CitX; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:RRD40692.1};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:RRD40692.1};
KW   Transferase {ECO:0000313|EMBL:RRD40692.1}.
SQ   SEQUENCE   430 AA;  49559 MW;  BA1CA1E5063D3627 CRC64;
     MNIGNFLNDR EKRVEYQKKL IEKYKKTLVV LKANFPGKNK NLPLADNIVD AISEEIDKLF
     EKNIIFRENF RNEEGKFFFY ILEGNAYNIK KSMIILEESH ELGRCADIDV HTPEGNVLSR
     KDIGNSFRKC FLCNDKAYNC VRSMKHSYEE LYNFLEEKYR NYIAHKFSLA ALEGLIYEVS
     AYPSFGLVSP VNTGSHKDMN FYTFLESGFA IEKAFYEITR IGYSDIELDT AFSIAREIGK
     KAEISMMRAT KNVNTHKGLI FLMGITVLAT ARNFYLGKNI EKIPELIRKI TKNILDDFKN
     IGNKENLTNG EKLYVKYGFT GIRGEVREGL TGIFDDILPF YDENLKCYSK NTVCSMTLIK
     LMNIINDSTI VHRHGIEMLS EVKKRTKSLI GISEKEKLEK FEKWCIENNI SPGGSADVLA
     VVIFLHNIYY
//
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