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Database: UniProt
Entry: A0A0P1GUQ3_9RHOB
LinkDB: A0A0P1GUQ3_9RHOB
Original site: A0A0P1GUQ3_9RHOB 
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
//
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