ID   A0A1M7I221_9RHOB        Unreviewed;       320 AA.
AC   A0A1M7I221;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Beta-methylmalyl-CoA/L-malyl-CoA lyase {ECO:0000313|EMBL:SHM34841.1};
GN   ORFNames=SAMN05444389_107156 {ECO:0000313|EMBL:SHM34841.1};
OS   Paracoccus solventivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=53463 {ECO:0000313|EMBL:SHM34841.1, ECO:0000313|Proteomes:UP000184444};
RN   [1] {ECO:0000313|EMBL:SHM34841.1, ECO:0000313|Proteomes:UP000184444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6637 {ECO:0000313|EMBL:SHM34841.1,
RC   ECO:0000313|Proteomes:UP000184444};
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};
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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DR   EMBL; FRCK01000007; SHM34841.1; -; Genomic_DNA.
DR   RefSeq; WP_073067179.1; NZ_FRCK01000007.1.
DR   AlphaFoldDB; A0A1M7I221; -.
DR   STRING; 53463.SAMN05444389_107156; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000184444; 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   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:SHM34841.1};
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          15..253
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   320 AA;  34331 MW;  7E7E0981221EEA4D CRC64;
     MSFRLQPAPP ARLNRCQLFG PGSRTQLFAK MAASAADVIN LDLEDSVAPD DKEQARKNII
     QAIGDIDWGN KTLSVRINGL DTPFWYRDVV DLLEQAGDRL DQIMIPKAGC AADIYAVDAL
     VTAIERAKGR KKPISFEVII ETAAGISHVE EIAASSPRLQ AMSLGAADFA ASMGMATTGI
     GGTQENYYMA RQGQKYWSDP WHWAQAAIVA ACRTHGVLPV DGPFGDFSDE EGFRAQALRS
     ATLGMVGKWA IHPSQVALAN EVFSPSEAAV AEAREIIAAM DQAQKSGAGA AVYKGRLVDI
     ASIRQAEVIV RQAEMIAAEA
//