ID   CITC_HAEIN              Reviewed;         335 AA.
AC   P44462;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 114.
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; OrderedLocusNames=HI_0025;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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;
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L42023; AAC21703.1; -; Genomic_DNA.
DR   PIR; F64043; F64043.
DR   RefSeq; NP_438198.1; NC_000907.1.
DR   RefSeq; WP_005668021.1; NC_000907.1.
DR   AlphaFoldDB; P44462; -.
DR   STRING; 71421.HI_0025; -.
DR   DNASU; 950918; -.
DR   EnsemblBacteria; AAC21703; AAC21703; HI_0025.
DR   KEGG; hin:HI_0025; -.
DR   PATRIC; fig|71421.8.peg.25; -.
DR   eggNOG; COG3053; Bacteria.
DR   HOGENOM; CLU_063190_0_0_6; -.
DR   OMA; YVFVLSE; -.
DR   PhylomeDB; P44462; -.
DR   BioCyc; HINF71421:G1GJ1-25-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IBA:GO_Central.
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   GO; GO:0036211; P:protein modification process; IBA:GO_Central.
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; 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; Reference proteome.
FT   CHAIN           1..335
FT                   /note="[Citrate [pro-3S]-lyase] ligase"
FT                   /id="PRO_0000089771"
FT   DOMAIN          1..131
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   335 AA;  38495 MW;  BF7CE241C725C8EC CRC64;
     MQFERISTEQ KKLSLIQTFL HQNALKLDEQ IEYFVVGYND NEQIVVCGGL AGNIIKCVAI
     DESLRGSGVA LQLITELVDL AYTLKRPHLF IYTKPEYATL FKSCGFYIIS DANPYVVLLE
     NSATRLQKQC SLWEKMRVDG NRIGSIVMNA NPFTLGHRYL IEQALQQCDH LHLFIVGEDA
     SQFSYTERFE MIQQGIFDLS NITLHSGSDY IISRATFPNY FLKDQLITDE SYFEIDLKLF
     RLHIAQALGI THRFVGTELN CPVTAEYNRQ MHYWLMDAEM NAPKINVIEI PRKTASNHII
     SASTVRKHLA EKNWAQLAEF VPMTTLNYLQ KCGRF