ID A0A1T0ARL4_9PAST Unreviewed; 230 AA.
AC A0A1T0ARL4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 08-OCT-2025, entry version 25.
DE RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000256|ARBA:ARBA00013186, ECO:0000256|NCBIfam:TIGR00760};
DE EC=5.1.3.4 {ECO:0000256|ARBA:ARBA00013186, ECO:0000256|NCBIfam:TIGR00760};
GN ORFNames=B0187_06825 {ECO:0000313|EMBL:OOR98968.1};
OS Haemophilus paracuniculus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pasteurellales; Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=734 {ECO:0000313|EMBL:OOR98968.1, ECO:0000313|Proteomes:UP000190867};
RN [1] {ECO:0000313|EMBL:OOR98968.1, ECO:0000313|Proteomes:UP000190867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 43573 {ECO:0000313|EMBL:OOR98968.1,
RC ECO:0000313|Proteomes:UP000190867};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Haemophilus paracuniculus CCUG 43573 type
RT strain.";
RL Submitted (FEB-2017) 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}.
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:OOR98968.1}.
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DR EMBL; MUYA01000008; OOR98968.1; -; Genomic_DNA.
DR RefSeq; WP_078237115.1; NZ_MUYA01000008.1.
DR AlphaFoldDB; A0A1T0ARL4; -.
DR STRING; 734.B0187_06825; -.
DR OrthoDB; 9786287at2; -.
DR Proteomes; UP000190867; 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-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019572; P:L-arabinose catabolic process; IEA:InterPro.
DR CDD; cd00398; Aldolase_II; 1.
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 InterPro; IPR004661; AraD.
DR NCBIfam; TIGR00760; araD; 1.
DR NCBIfam; NF006047; PRK08193.1; 1.
DR NCBIfam; NF009002; PRK12347.1; 1.
DR NCBIfam; NF009003; PRK12348.1; 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:UP000190867};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 7..197
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 230 AA; 25867 MW; AA5781148FA9355E CRC64;
MLKELRERVL KANLELPKYK LVTFTWGNVS ELDRETGLVA IKPSGVEYDV MTADDIVIVD
LQGNRVWGDK KPSSDTPTHL ELYRQFPEIG GVVHTHSRHA TAWAQAGEDI LALGTTQGDY
FYGSVPCTRR MTPEEIAGEY ELETGKVIVE TFRKRGIEAK AVPGVLVHSH GPFTWGKDAF
DAVHNSVVLE EVAYMNFISH QIRPNIGSMQ QELLDKHYLR KHGANAYYGQ
//
