ID   A0A1H2MWA2_9PSED        Unreviewed;       267 AA.
AC   A0A1H2MWA2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=(S)-citramalyl-CoA lyase {ECO:0000313|EMBL:SDU97527.1};
GN   ORFNames=SAMN05216202_2520 {ECO:0000313|EMBL:SDU97527.1};
OS   Pseudomonas mucidolens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=46679 {ECO:0000313|EMBL:SDU97527.1, ECO:0000313|Proteomes:UP000198600};
RN   [1] {ECO:0000313|Proteomes:UP000198600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 2223 {ECO:0000313|Proteomes:UP000198600};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; LT629802; SDU97527.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2MWA2; -.
DR   STRING; 46679.SAMN05216202_2520; -.
DR   Proteomes; UP000198600; Chromosome i.
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:SDU97527.1};
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          2..209
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   267 AA;  28571 MW;  BE9A6B0B05A8195A CRC64;
     MRSALFVPGD RPERYEKALA SGADRVIVDF EDAVEEGSKS SARESLGEYL LSHPQATVLV
     RVNSPGHVQH EADLAFCKEH QGVIGIMLPK TETRAQLANA AETRKPILPI IETALGVMNL
     PELCSVPGLE RLCFGAIDMA LDLGLKDGSP GALTVLDHLR VSVIVQSRIY GLASPLDGVF
     PSINDLPGLT RAVQTALEMG FGGVLCIHPK QVVVIHEALT PEADEVSWAN RVLSAAETQG
     GAFKLDGQMI DAPVLSRARR IINALSN
//