ID   F0M8N7_PSEPM            Unreviewed;       236 AA.
AC   F0M8N7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   OrderedLocusNames=Asphe3_03650 {ECO:0000313|EMBL:ADX71580.1};
OS   Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG
OS   23796 / Sphe3) (Arthrobacter phenanthrenivorans).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Pseudarthrobacter.
OX   NCBI_TaxID=930171 {ECO:0000313|EMBL:ADX71580.1, ECO:0000313|Proteomes:UP000008639};
RN   [1] {ECO:0000313|EMBL:ADX71580.1, ECO:0000313|Proteomes:UP000008639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3
RC   {ECO:0000313|Proteomes:UP000008639};
RX   PubMed=21677849; DOI=10.4056/sigs.1393494;
RA   Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A.,
RA   Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L., Pitluck S.,
RA   Chen A., Palaniappan K., Markowitz V., Bristow J., Velentzas A.D.,
RA   Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT   "Complete genome sequence of Arthrobacter phenanthrenivorans type strain
RT   (Sphe3).";
RL   Stand. Genomic Sci. 4:123-130(2011).
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; CP002379; ADX71580.1; -; Genomic_DNA.
DR   RefSeq; WP_013599522.1; NC_015145.1.
DR   AlphaFoldDB; F0M8N7; -.
DR   STRING; 930171.Asphe3_03650; -.
DR   KEGG; apn:Asphe3_03650; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_006033_3_0_11; -.
DR   OrthoDB; 9786287at2; -.
DR   Proteomes; UP000008639; Chromosome.
DR   GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-EC.
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   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   Isomerase {ECO:0000313|EMBL:ADX71580.1}.
FT   DOMAIN          19..207
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   236 AA;  25201 MW;  770EDD51ED7880B3 CRC64;
     MSSEILGTEI LGTIARIREE VCALHAELTR YQLVVWTAGN VSARVPGQEL MVIKPSGVSY
     QDLTPEQMVV TDLYGVPVAG DATGEWGNPA LSPSSDTAAH AYVYRHMPEV GGVVHTHSTY
     ATAWAARGEA IPCVLTMMSD EFGGEIPVGP FALIGDDSIG HGIVETLKNS NSPAVLMQNH
     GPFTIGKDAK SAVKAAVMCE EVARTVHIAR QLGDPIAIDQ GHIESLYARY QNVYGQ
//