ID A0A0C1IXY9_9RHOB Unreviewed; 325 AA.
AC A0A0C1IXY9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Malyl-CoA lyase {ECO:0000313|EMBL:KIC40637.1};
GN ORFNames=RA27_12770 {ECO:0000313|EMBL:KIC40637.1};
OS Ruegeria sp. ANG-R.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577903 {ECO:0000313|EMBL:KIC40637.1, ECO:0000313|Proteomes:UP000031318};
RN [1] {ECO:0000313|Proteomes:UP000031318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-R {ECO:0000313|Proteomes:UP000031318};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIC40637.1}.
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DR EMBL; JWLJ01000004; KIC40637.1; -; Genomic_DNA.
DR RefSeq; WP_039539428.1; NZ_JWLJ01000004.1.
DR AlphaFoldDB; A0A0C1IXY9; -.
DR STRING; 1577903.RA27_12770; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000031318; 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:KIC40637.1};
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 16..259
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 325 AA; 35343 MW; 582D68E419E609FE CRC64;
MSFFAIDQAT ARLNRSELAV PGSQPSMFEK AAQSDVDVIF LDLEDAVAPD EKEQARKNII
RALNDIDWGS KTMSVRINGL DTHYMYRDVV DVVEQAGERL DLIMIPKVGT AADVYAVDMM
VTQIEDAMGY KNRIGFEHII ETALGMQNVS EIAAASKRNE SLHFGVADYA ASTRARTTII
GGVNPDYSVL TDPDHGANRA THWGDMWHYA LARMVVAARA NGLRPIDGPF GDFQDPEGYK
AAAKRAAVLG CEGKWAIHPS QIALANEVMS PSEAEVTKAQ RILVAMSEAE TAGKGAVSLD
GRLIDYASIR QAEVMVEKAR QIAAA
//
