ID A8U148_9PROT Unreviewed; 285 AA.
AC A8U148;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Citrate lyase {ECO:0000313|EMBL:EDP61975.1};
GN ORFNames=BAL199_10280 {ECO:0000313|EMBL:EDP61975.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP61975.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP61975.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP61975.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP61975.1}.
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DR EMBL; ABHC01000025; EDP61975.1; -; Genomic_DNA.
DR AlphaFoldDB; A8U148; -.
DR STRING; 331869.BAL199_10280; -.
DR eggNOG; COG2301; Bacteria.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000003417; Unassembled WGS sequence.
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:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 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 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EDP61975.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000003417}.
FT DOMAIN 10..223
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 285 AA; 30960 MW; E6B8E046D325A42A CRC64;
MTERAVRPRR SFIFAPGNKP EMFPKALKVG ADIMCVDLED AIAPQHKAEA RTTTLGWFAQ
AELDGEVEAM VRINPPRTPD GMRDIDAILS SPKAPPALML PKVKTPGEIT ALAELFDEFK
IAARLHVIIE TNEALEAAWD IARVSDRIDA LFFGGVDMAA DLRCRNSWAA LQYTRSRVVH
AAAGAGVDVI DVPYLDLNDM DGMRAEAEAA AELGFSGKGS IHPKQVPVLN AVFTPSEAEV
AYAQKIIFAF EQADSGLVVV DGKLMEKPVL RSMYRVLARA GQASN
//