ID F0NTM3_LACHH Unreviewed; 293 AA.
AC F0NTM3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Citrate lyase beta-chain {ECO:0000313|EMBL:ADX70397.1};
GN OrderedLocusNames=LBHH_1197 {ECO:0000313|EMBL:ADX70397.1};
OS Lactobacillus helveticus (strain H10).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=767462 {ECO:0000313|EMBL:ADX70397.1, ECO:0000313|Proteomes:UP000008640};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H10;
RA Zhang H., Zhao W., Chen Y., Sun Z., Sun T., Meng H.;
RT "Complete genome sequence of Lactobacillus helveticus strain H10.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADX70397.1, ECO:0000313|Proteomes:UP000008640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H10 {ECO:0000313|EMBL:ADX70397.1,
RC ECO:0000313|Proteomes:UP000008640};
RX PubMed=21398542; DOI=10.1128/JB.00166-11;
RA Zhao W., Chen Y., Sun Z., Wang J., Zhou Z., Sun T., Wang L., Chen W.,
RA Zhang H.;
RT "Complete genome sequence of Lactobacillus helveticus H10.";
RL J. Bacteriol. 193:2666-2667(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; CP002429; ADX70397.1; -; Genomic_DNA.
DR AlphaFoldDB; F0NTM3; -.
DR KEGG; lhl:LBHH_1197; -.
DR PATRIC; fig|767462.3.peg.1360; -.
DR HOGENOM; CLU_044864_0_0_9; -.
DR Proteomes; UP000008640; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ADX70397.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2}.
FT DOMAIN 1..218
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 293 AA; 32201 MW; DE27C81F1E81BEF1 CRC64;
MMFVPGNNPA MIKDAGIYGA DSIMLDLEDS VSLTEKDAAR MLVYEAIKTV DFGGSEIVVR
VNGQDTPFYD EDVRAMVKAG VDVIRLPKTE SAAMIQKLVK DIEHWEDEYG IEKGSIGVMA
AIESAKGVLN APEIATATPL MMGLAVSGED YTADMHTHRY PDGRELEFAR NMVLQAARAA
DVYAFDTVFS NMKDTEGFYR ETNYIHELGY DGKSLVNPRQ IAMVNKVFNP TKEEIEQAKN
VENAIREAKA KGSGVISLNG KMVDKPVVEK ATRVLETAKA SNLIDEEGNY IGE
//