ID   A0A0F2RX02_9RHOB        Unreviewed;       262 AA.
AC   A0A0F2RX02;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Aldolase {ECO:0000313|EMBL:KJS43128.1};
GN   ORFNames=VR71_11745 {ECO:0000313|EMBL:KJS43128.1};
OS   Roseovarius sp. BRH_c41.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1629709 {ECO:0000313|EMBL:KJS43128.1, ECO:0000313|Proteomes:UP000033676};
RN   [1] {ECO:0000313|EMBL:KJS43128.1, ECO:0000313|Proteomes:UP000033676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c41 {ECO:0000313|EMBL:KJS43128.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-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}.
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:KJS43128.1}.
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DR   EMBL; LADY01000037; KJS43128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2RX02; -.
DR   PATRIC; fig|1629709.5.peg.937; -.
DR   Proteomes; UP000033676; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   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          9..207
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   262 AA;  26866 MW;  580725B309F17903 CRC64;
     MVSSIATPLF VPASKPERFV KAAARGADAV ILDLEDAVAA ADKDTARAAL NAEFTDLPVI
     VRINAIGTPW HAADLAAVSG KGFAAVILPK SETAETVAQV VAALPGLPVI ALIESALGLA
     NARAIAAVDG VARLAFGSVD FCADLGCAHL RDILLPARSE LVLASRLGGI AAPIDGVTVQ
     LDDPAVTRDD AGHARDLGMT GKLCIHPKQI AEVKRAFAPS EDEISWAKRV LASGDGAVAV
     DGAMVDEPVR IRARAILAAV PE
//