ID Q1JLM0_STRPC Unreviewed; 350 AA.
AC Q1JLM0;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
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:ABF32199.1};
GN OrderedLocusNames=MGAS9429_Spy1012 {ECO:0000313|EMBL:ABF32199.1};
OS Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370551 {ECO:0000313|EMBL:ABF32199.1, ECO:0000313|Proteomes:UP000002433};
RN [1] {ECO:0000313|EMBL:ABF32199.1, ECO:0000313|Proteomes:UP000002433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS9429 {ECO:0000313|EMBL:ABF32199.1,
RC ECO:0000313|Proteomes:UP000002433};
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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}.
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DR EMBL; CP000259; ABF32199.1; -; Genomic_DNA.
DR RefSeq; WP_002989752.1; NC_008021.1.
DR AlphaFoldDB; Q1JLM0; -.
DR KEGG; spk:MGAS9429_Spy1012; -.
DR HOGENOM; CLU_063190_0_0_9; -.
DR Proteomes; UP000002433; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR005751};
KW Ligase {ECO:0000256|PIRNR:PIRNR005751, ECO:0000313|EMBL:ABF32199.1};
KW Lyase {ECO:0000313|EMBL:ABF32199.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR005751}.
FT DOMAIN 1..140
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 350 AA; 39507 MW; C7C577F5CD45038F CRC64;
MPYYTVSKVF PSDKTTMASV KNLLHQEGIR LDAHLDYTCA IMNAQNDVIA TGSYFGNSLR
CLCVSSAYQG EGLLNRIVSH LIDEEYALGN YHLFVYTKTS SAAFFKDLGF TEIVHIDNHI
SFLENKKTGF QDYLMTLNKP EQTPGKVAAI VINANPFTLG HQFLVEKAAR ENDWVHLFMV
SEDQSLVPFS VRKMLIQEGL RHLDNIIFHE TGPYLISQAT FPAYFQTEDN DVIKSQALLD
TAIFLKIAQT LQITKRYVGE EPTSRVTAIY NEIMAEQLQQ AGILLDILPR KAINQQQDPI
SASTARQALK DNDWDLLAKL LPKTSLDYFC SLEAQPIIKK IQATSSVKHY
//
