ID A0A1G8LUV8_9RHOB Unreviewed; 229 AA.
AC A0A1G8LUV8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-OCT-2025, entry version 22.
DE RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000256|ARBA:ARBA00013186};
DE EC=5.1.3.4 {ECO:0000256|ARBA:ARBA00013186};
GN ORFNames=SAMN04487993_100714 {ECO:0000313|EMBL:SDI59458.1};
OS Salipiger marinus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Salipiger.
OX NCBI_TaxID=555512 {ECO:0000313|EMBL:SDI59458.1, ECO:0000313|Proteomes:UP000199093};
RN [1] {ECO:0000313|EMBL:SDI59458.1, ECO:0000313|Proteomes:UP000199093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26424 {ECO:0000313|EMBL:SDI59458.1,
RC ECO:0000313|Proteomes:UP000199093};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226;
CC EC=5.1.3.4; Evidence={ECO:0000256|ARBA:ARBA00001726};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC subfamily. {ECO:0000256|ARBA:ARBA00010037}.
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DR EMBL; FNEJ01000007; SDI59458.1; -; Genomic_DNA.
DR RefSeq; WP_089846159.1; NZ_FNEJ01000007.1.
DR AlphaFoldDB; A0A1G8LUV8; -.
DR STRING; 555512.SAMN04487993_100714; -.
DR OrthoDB; 5291399at2; -.
DR Proteomes; UP000199093; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:TreeGrafter.
DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019323; P:pentose catabolic process; IEA:TreeGrafter.
DR FunFam; 3.40.225.10:FF:000001; L-ribulose-5-phosphate 4-epimerase UlaF; 1.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR InterPro; IPR050197; Aldolase_class_II_sugar_metab.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR NCBIfam; NF006047; PRK08193.1; 1.
DR PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR22789:SF8; L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE SGBE; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000199093};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 8..196
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 229 AA; 24554 MW; 5CD794BBB34786AD CRC64;
MTLAALRQAV LDANLATVQH GLVKATFGNA SGIDRASGRI AIKPSGVPYD DMTPDHMVIT
DLDGGTLDNR YRPSSDLDTH LVLYRAFPTI GAIIHTHSTY ATIMAQARRP IPPLGTTHAD
YFHGTIPVTR DLTPEEITTR YVESTGEVIV ETVGAGDPLA IPAVLVAGHG PFVWGRDPEE
AVLNALILEE VAKMAWHGAA LDASPPPISQ ALLDRHFLRK HGANATYGQ
//
