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Database: UniProt
Entry: A8U148_9PROT
LinkDB: A8U148_9PROT
Original site: A8U148_9PROT 
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
//
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