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Database: UniProt
Entry: C5B715_EDWI9
LinkDB: C5B715_EDWI9
Original site: C5B715_EDWI9 
ID   C5B715_EDWI9            Unreviewed;       358 AA.
AC   C5B715;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=[Citrate [pro-3S]-lyase] ligase {ECO:0000256|PIRNR:PIRNR005751};
DE            EC=6.2.1.22 {ECO:0000256|PIRNR:PIRNR005751};
GN   OrderedLocusNames=NT01EI_0234 {ECO:0000313|EMBL:ACR67477.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67477.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67477.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67477.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated with
RT   a Natural Channel Catfish Outbreak of Enteric Septicemia of Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
CC   -!- FUNCTION: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-
CC       dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
CC       {ECO:0000256|PIRNR:PIRNR005751}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate
CC         lyase ACP] + AMP + diphosphate; Xref=Rhea:RHEA:23788, Rhea:RHEA-
CC         COMP:10158, Rhea:RHEA-COMP:13710, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82683,
CC         ChEBI:CHEBI:137976, ChEBI:CHEBI:456215; EC=6.2.1.22;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005751};
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DR   EMBL; CP001600; ACR67477.1; -; Genomic_DNA.
DR   RefSeq; WP_015869686.1; NC_012779.2.
DR   AlphaFoldDB; C5B715; -.
DR   STRING; 67780.B6E78_12290; -.
DR   GeneID; 69537334; -.
DR   KEGG; eic:NT01EI_0234; -.
DR   PATRIC; fig|634503.3.peg.210; -.
DR   HOGENOM; CLU_063190_0_0_6; -.
DR   OMA; YVFVLSE; -.
DR   OrthoDB; 9779753at2; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02169; Citrate_lyase_ligase; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR005216; Citrate_lyase_ligase.
DR   InterPro; IPR013166; Citrate_lyase_ligase_C.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00124; cit_ly_ligase; 1.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   PANTHER; PTHR40599; [CITRATE [PRO-3S]-LYASE] LIGASE; 1.
DR   PANTHER; PTHR40599:SF1; [CITRATE [PRO-3S]-LYASE] LIGASE; 1.
DR   Pfam; PF08218; Citrate_ly_lig; 1.
DR   PIRSF; PIRSF005751; Acet_citr_lig; 1.
DR   SMART; SM00764; Citrate_ly_lig; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR005751};
KW   Ligase {ECO:0000256|PIRNR:PIRNR005751, ECO:0000313|EMBL:ACR67477.1};
KW   Lyase {ECO:0000313|EMBL:ACR67477.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR005751}.
FT   DOMAIN          1..135
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   358 AA;  40277 MW;  22488EAD94E05E43 CRC64;
     MFSNTVFTQI KRSEQKRIAD ITHFLRENGL NIDTSVEIFI CAQRDNKIIA CGGIAGDIIK
     CVAISAAARG EGLALTLATE LVNLAYELGR NNLFIYTKEE NEGMFHQCGF STITRVPGIM
     VLMENSKVRL QRYAETLVTL RHPGKKIGAI VMNANPFTNG HRYLVRQAAS QCDWLHLFLV
     REDTSRFPYE DRLALVRSGV SDIANLTLHP GSEYIISRAT FPCYFIKEQG VADNCYTEID
     IKIFRQYLAP ALGITHRFVG TEPFCPVTAK YNQDMRYWLE TPALPYPPIH LVEVARLTYH
     NTPISASWVR KLLVRKDIPA ITPLVPNATR AYLARLIASI PAGVERRSQE SVLVTGDK
//
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