ID   CITC_KLEPN              Reviewed;         342 AA.
AC   P45410;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=[Citrate [pro-3S]-lyase] ligase;
DE            EC=6.2.1.22;
DE   AltName: Full=Acetate:SH-citrate lyase ligase;
DE   AltName: Full=Citrate lyase synthetase;
GN   Name=citC;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13882 / NBRC 13541 / NCTC 8172;
RX   PubMed=7830578; DOI=10.1111/j.1365-2958.1994.tb01295.x;
RA   Bott M., Dimroth P.;
RT   "Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase:
RT   localization, sequencing, and expression.";
RL   Mol. Microbiol. 14:347-356(1994).
CC   -!- FUNCTION: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-
CC       dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
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;
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DR   EMBL; X79817; CAA56214.1; -; Genomic_DNA.
DR   PIR; S60773; S60773.
DR   RefSeq; WP_004222626.1; NZ_WYAL01000016.1.
DR   AlphaFoldDB; P45410; -.
DR   SMR; P45410; -.
DR   BioCyc; MetaCyc:MON-17001; -.
DR   GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd02169; Citrate_lyase_ligase; 1.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR40599; PTHR40599; 1.
DR   Pfam; PF00583; Acetyltransf_1; 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; SSF55729; 1.
DR   TIGRFAMs; TIGR00124; cit_ly_ligase; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..342
FT                   /note="[Citrate [pro-3S]-lyase] ligase"
FT                   /id="PRO_0000089772"
FT   DOMAIN          1..127
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   342 AA;  38477 MW;  5745C4677B6E3678 CRC64;
     MTLILKRVQL LKDKPRREAI DRFLRQHQLS LEADCEMAII AEYQQRLVGC GAIAGNVLKC
     IAIDPSLQGE GLSLKLLTEL LTLAYELGRS ELFLFTKPCN AALFSGAGFW PIAQAGDRAV
     LMENSRERLT RYCRQLAMYR QPGRKIGAIV MNANPFTLGH RWLVEQAASQ CDWLHLFVVK
     EDASCFSYHD RFKLIEQGIT GIDKVTLHPG SAYLISRATF PGYFLKEQGV VDDCHSQIDL
     QLFRERLAPA LQITHRFVGT EPLCPLTRNY NQRMKSLLEA PGDAPPIEVV ELARIEKNGG
     PVSASRVREL YRQRNWQAVA ALVPPGTLSF LMQLAESEHQ TA