ID G5K376_9STRE Unreviewed; 349 AA.
AC G5K376;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=[Citrate [pro-3S]-lyase] ligase {ECO:0000256|PIRNR:PIRNR005751};
DE EC=6.2.1.22 {ECO:0000256|PIRNR:PIRNR005751};
GN Name=citC {ECO:0000313|EMBL:EHI69398.1};
GN ORFNames=STRIC_1244 {ECO:0000313|EMBL:EHI69398.1};
OS Streptococcus ictaluri 707-05.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764299 {ECO:0000313|EMBL:EHI69398.1, ECO:0000313|Proteomes:UP000003330};
RN [1] {ECO:0000313|EMBL:EHI69398.1, ECO:0000313|Proteomes:UP000003330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=707-05 {ECO:0000313|EMBL:EHI69398.1,
RC ECO:0000313|Proteomes:UP000003330};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
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};
CC -!- SIMILARITY: Belongs to the acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00008694}.
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:EHI69398.1}.
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DR EMBL; AEUX02000006; EHI69398.1; -; Genomic_DNA.
DR RefSeq; WP_008088770.1; NZ_AEUX02000006.1.
DR AlphaFoldDB; G5K376; -.
DR STRING; 764299.STRIC_1244; -.
DR eggNOG; COG3053; Bacteria.
DR OrthoDB; 9779753at2; -.
DR Proteomes; UP000003330; Unassembled WGS sequence.
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 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; IPR000182; GNAT_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00124; cit_ly_ligase; 1.
DR PANTHER; PTHR40599; [CITRATE [PRO-3S]-LYASE] LIGASE; 1.
DR PANTHER; PTHR40599:SF1; [CITRATE [PRO-3S]-LYASE] LIGASE; 1.
DR Pfam; PF13673; Acetyltransf_10; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR005751};
KW Ligase {ECO:0000256|PIRNR:PIRNR005751, ECO:0000313|EMBL:EHI69398.1};
KW Lyase {ECO:0000313|EMBL:EHI69398.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR005751};
KW Reference proteome {ECO:0000313|Proteomes:UP000003330}.
FT DOMAIN 1..139
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 349 AA; 39462 MW; 650280EC44AB40B3 CRC64;
MSSDLIQRVF PYDRQAIKAV NQLLEQEKIK RDPNLDYTCA IFDESQRVIA TGSLFRNSLR
CLAVDFRYQG EGLLNKIVSH LISEASDRGD YPLFVYTKIS AVPFFESLGF QEIVRVDEDL
SFLESQRDGF ATYLKHLATS KTTSQNSAAV VINANPFTLG HLYLIEKAAS ENQALHLFMV
SQDSSLIPFT VRRDLILKGT AHLKNICYHE TGDYLISQAT FPSYFQKDQL AAIKSQAKLD
ATIFSQIAKQ LGITKRYIGE EPSSLVTNHY NQIMLDFLPK VGISVKKYDR LKLPDGRPIS
ASLVRQALKE ENHALFSNLL PQTSLDYFLS DEATTIIDKL KATKDLTHY
//
