ID A0A0P1IFH1_9RHOB Unreviewed; 320 AA.
AC A0A0P1IFH1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Malyl-CoA lyase {ECO:0000313|EMBL:CUK10073.1};
DE EC=4.1.3.24 {ECO:0000313|EMBL:CUK10073.1};
GN Name=mcl1_1 {ECO:0000313|EMBL:CUK10073.1};
GN ORFNames=RUE5091_03266 {ECO:0000313|EMBL:CUK10073.1};
OS Ruegeria denitrificans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1715692 {ECO:0000313|EMBL:CUK10073.1, ECO:0000313|Proteomes:UP000051260};
RN [1] {ECO:0000313|EMBL:CUK10073.1, ECO:0000313|Proteomes:UP000051260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5091 {ECO:0000313|EMBL:CUK10073.1,
RC ECO:0000313|Proteomes:UP000051260};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYUD01000010; CUK10073.1; -; Genomic_DNA.
DR RefSeq; WP_058282935.1; NZ_CYUD01000010.1.
DR AlphaFoldDB; A0A0P1IFH1; -.
DR STRING; 1715692.RUE5091_03266; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000051260; Unassembled WGS sequence.
DR GO; GO:0043959; F:L-erythro-3-methylmalyl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0050083; F:malyl-CoA lyase activity; IEA:UniProtKB-EC.
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:CUK10073.1};
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; 34281 MW; 158E8D9CDE27880E CRC64;
MSFRLQPAAP ARPNRCQLFG PGSNTKLFPK MAASAADVIN LDLEDSVAPS DKDIARANVI
EALNTVDWGN KHMSVRINGL DTPYWYRDVV DLLEQAGDRL DQIMIPKVGC AADVYAVDAL
VTAIERAKGR SKPISFEVII ESAAGIAHVE EIAASSPRMQ AMSLGAADFA ASMGMQTTGI
GGTQENYYML RDGEKHWSDP WHWAQAAIVA ACRTHGVLPV DGPFGDFSDD EGYIAQAKRS
ATLGMVGKWA IHPKQIALAN QVFTPSDEAV SEAREILAAM EQAKANGEGA TVYKGRLVDI
ASIKQAEVIV AQAELIAANG
//
