ID A0A0P1GUQ3_9RHOB Unreviewed; 320 AA.
AC A0A0P1GUQ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Malyl-CoA lyase {ECO:0000313|EMBL:CUH78810.1};
DE EC=4.1.3.24 {ECO:0000313|EMBL:CUH78810.1};
GN Name=mcl1 {ECO:0000313|EMBL:CUH78810.1};
GN ORFNames=TRM7557_02052 {ECO:0000313|EMBL:CUH78810.1};
OS Tritonibacter multivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH78810.1, ECO:0000313|Proteomes:UP000052022};
RN [1] {ECO:0000313|EMBL:CUH78810.1, ECO:0000313|Proteomes:UP000052022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH78810.1,
RC ECO:0000313|Proteomes:UP000052022};
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; CYSD01000033; CUH78810.1; -; Genomic_DNA.
DR RefSeq; WP_058290111.1; NZ_JAQIPA010000012.1.
DR AlphaFoldDB; A0A0P1GUQ3; -.
DR STRING; 928856.SAMN04488049_110134; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000052022; 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:CUH78810.1};
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:UP000052022}.
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; 34220 MW; A25CB5C42EFA0F12 CRC64;
MSFRIQPAAP ARPNRCQLFG PGSNTKLFPK MAASAADVIN LDLEDSVAPS DKDTARANVI
EALNTVDWGN KYMSVRINGL DTPYWYRDVV DLLEQAGDRI DQIMIPKVGC AEDVYAVDAL
VTAIEAAKGR TKPVSFEVII ESAAGIAHVE AIAASSPRLQ AMSLGAADFA ASMGMQTTGI
GGTQENYYML REGAKHWSDP WHWAQAAIVA ACRTHGILPV DGPFGDFSDD DGYIAQAKRS
ATLGMVGKWA IHPKQIALAN EVFTPSEDAV TEAREILAAM EQAKANGEGA TVYKGRLVDI
ASIKQAEVIV AQAELIAQNG
//