ID W4Q6W9_9BACI Unreviewed; 236 AA.
AC W4Q6W9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000256|ARBA:ARBA00013186};
DE EC=5.1.3.4 {ECO:0000256|ARBA:ARBA00013186};
DE AltName: Full=Phosphoribulose isomerase {ECO:0000256|ARBA:ARBA00032206};
GN ORFNames=JCM9140_3909 {ECO:0000313|EMBL:GAE27752.1};
OS Halalkalibacter wakoensis JCM 9140.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=1236970 {ECO:0000313|EMBL:GAE27752.1, ECO:0000313|Proteomes:UP000018890};
RN [1] {ECO:0000313|EMBL:GAE27752.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9140 {ECO:0000313|EMBL:GAE27752.1};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT hemicellulosilyticus JCM 9152T.";
RL Genome Announc. 2:e01258-13(2014).
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:GAE27752.1}.
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DR EMBL; BAUT01000063; GAE27752.1; -; Genomic_DNA.
DR RefSeq; WP_034749449.1; NZ_BAZN01000063.1.
DR AlphaFoldDB; W4Q6W9; -.
DR STRING; 1236970.JCM9140_3909; -.
DR OrthoDB; 9786287at2; -.
DR Proteomes; UP000018890; Unassembled WGS sequence.
DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000018890}.
FT DOMAIN 7..195
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 236 AA; 26532 MW; 8E38CF761FC6F0CD CRC64;
MLESLKMQVL EANLALPKYG LVTFTWGNVS GFDKEQGLVV IKPSGVPYEE LTVEKLVVLD
LEGTIVEGEL KPSSDTPTHL VLYRNFPDIG GIVHTHSPWA TSWAQAGKPI QALGTTQADY
FYGTVPCTRR MTEEEIQGEY ELETGNVIVE TFEEIDPMQI PSVLVHSHAP FNWGKDPHEA
VHNAVVLEEV AKMNFHTYQI NPEIPTMDQT LLNKHYLRKH GGNAYYGQQN KRELSK
//