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Database: UniProt
Entry: A0A1M5PVX2_9BURK
LinkDB: A0A1M5PVX2_9BURK
Original site: A0A1M5PVX2_9BURK 
ID   A0A1M5PVX2_9BURK        Unreviewed;       331 AA.
AC   A0A1M5PVX2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Beta-methylmalyl-CoA/L-malyl-CoA lyase {ECO:0000313|EMBL:SHH05661.1};
GN   ORFNames=SAMN04488135_10266 {ECO:0000313|EMBL:SHH05661.1};
OS   Pollutimonas bauzanensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pollutimonas.
OX   NCBI_TaxID=658167 {ECO:0000313|EMBL:SHH05661.1, ECO:0000313|Proteomes:UP000184226};
RN   [1] {ECO:0000313|EMBL:SHH05661.1, ECO:0000313|Proteomes:UP000184226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10190 {ECO:0000313|EMBL:SHH05661.1,
RC   ECO:0000313|Proteomes:UP000184226};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; FQXE01000002; SHH05661.1; -; Genomic_DNA.
DR   RefSeq; WP_073101729.1; NZ_FQXE01000002.1.
DR   AlphaFoldDB; A0A1M5PVX2; -.
DR   STRING; 658167.SAMN04488135_10266; -.
DR   OrthoDB; 348111at2; -.
DR   Proteomes; UP000184226; 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: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:SHH05661.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184226}.
FT   DOMAIN          17..260
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   331 AA;  35572 MW;  5B4BFE57A5F1AD56 CRC64;
     MHASATAGSP RTRRLQRSCL AVPATSEVFF EKAAKGEADE VFLDLEDAVS PGEKERARHL
     AIAAINDIDW QDKIVAVRVN GLDTPWGYRD IVDVVEQCPR LDLIMLPKAG SAADVQFVDT
     LLSGIELAIG RRDPIGIEAL IESAMGMVNA AKIAQASPRL EALIFGVGDY MIDMQTSDMR
     MGSLNQDYAV VNDIDGAQAA SSYLANHWHY AQSRIATVCR AYGLRPIDGP YTDFSDMAGY
     QASACRGRAL GFEGKWAIHP SQVAQANTAF TPSAQRVSWA ARVAQAMDDA VGQGRGAINL
     DGELIDMAHV KLAANIRRRA ALAAGNPNES A
//
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