CITE_HAEIN
ID CITE_HAEIN Reviewed; 291 AA.
AC P44460;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Citrate lyase subunit beta;
DE Short=Citrase beta chain;
DE EC=4.1.3.6;
DE AltName: Full=Citrate (pro-3S)-lyase subunit beta;
DE AltName: Full=Citryl-CoA lyase subunit;
DE EC=4.1.3.34;
GN Name=citE; OrderedLocusNames=HI_0023;
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: Represents a citryl-ACP lyase. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = acetate + oxaloacetate; Xref=Rhea:RHEA:10760,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089; EC=4.1.3.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-citryl-CoA = acetyl-CoA + oxaloacetate;
CC Xref=Rhea:RHEA:20812, ChEBI:CHEBI:16452, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57321; EC=4.1.3.34;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta,gamma)6.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. Citrate lyase
CC beta subunit subfamily. {ECO:0000305}.
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; AAC21701.1; -; Genomic_DNA.
DR PIR; D64043; D64043.
DR RefSeq; NP_438196.2; NC_000907.1.
DR RefSeq; WP_005693883.1; NC_000907.1.
DR AlphaFoldDB; P44460; -.
DR SMR; P44460; -.
DR STRING; 71421.HI_0023; -.
DR EnsemblBacteria; AAC21701; AAC21701; HI_0023.
DR KEGG; hin:HI_0023; -.
DR PATRIC; fig|71421.8.peg.23; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_0_6; -.
DR OMA; AWLFCPA; -.
DR PhylomeDB; P44460; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009346; C:ATP-independent citrate lyase complex; IEA:InterPro.
DR GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0008816; F:citryl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR InterPro; IPR006475; Citrate_lyase_beta_bac.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR01588; citE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..291
FT /note="Citrate lyase subunit beta"
FT /id="PRO_0000089758"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 291 AA; 31855 MW; 9DB1B9D202CF221F CRC64;
MKLRRSMLFV PGSNAAMLSN SFIYKPDSIM FDLEDAVALK EKDSARLLVA HALQHPLYKE
IETVVRVNPL DSEFGLLDLN SVVRAGVDVV RMPKTESAQD VLDMDHAITE IEKACGREAG
STKMLAAIES PLGITQANQI AFASKRLIGI ALGAEDYVRN LKTERSPEGI ELLFARCSIL
QAARAAGIQA FDTVYSNANN EEGFLKEAAL IKQLGFDGKS LINPRQIELL HNLFAPTQKD
VEQAKRIIEA AVEAERQGAG VVSLNGKMID APIIDRAKLV LERAKSGIRE E
