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Database: UniProt
Entry: A0A068NNH0_9ACTO
LinkDB: A0A068NNH0_9ACTO
Original site: A0A068NNH0_9ACTO 
ID   A0A068NNH0_9ACTO        Unreviewed;       222 AA.
AC   A0A068NNH0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=FB03_07205 {ECO:0000313|EMBL:AIE83069.1};
OS   Actinotignum schaalii.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinotignum.
OX   NCBI_TaxID=59505 {ECO:0000313|EMBL:AIE83069.1, ECO:0000313|Proteomes:UP000035032};
RN   [1] {ECO:0000313|EMBL:AIE83069.1, ECO:0000313|Proteomes:UP000035032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE83069.1,
RC   ECO:0000313|Proteomes:UP000035032};
RX   PubMed=25189588;
RA   Kristiansen R., Dueholm M.S., Bank S., Nielsen P.H., Karst S.M.,
RA   Cattoir V., Lienhard R., Grisold A.J., Olsen A.B., Reinhard M., Soby K.M.,
RA   Christensen J.J., Prag J., Thomsen T.R.;
RT   "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG 27420.";
RL   Genome Announc. 2:e00880-14(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}.
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DR   EMBL; CP008802; AIE83069.1; -; Genomic_DNA.
DR   RefSeq; WP_026429007.1; NZ_JARBHM010000002.1.
DR   AlphaFoldDB; A0A068NNH0; -.
DR   GeneID; 81702190; -.
DR   KEGG; asg:FB03_07205; -.
DR   Proteomes; UP000035032; 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:AIE83069.1}.
FT   DOMAIN          7..184
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   222 AA;  23775 MW;  F29AF8C40A82A8C2 CRC64;
     MLEQLREEVC AGNLELPRHG LVAWTGGNLS AIDEETGYIV IKPSGMRYED MTPKDMVVVA
     PDGRVVEGEH GPSSDTSSHL YIYQHKKDVK SVIHTHSRYA TAFAAVGKPI PCCLTAIADE
     FGGPIPCGGY ARIGSDEIGA EVIRSIGDSP AILMKQHGVF TIGSSIAKAL QAAVMVEDVA
     RTVAIATGLG QIEDLPAEEV LANHDRYQNR YGTMNASLGV RQ
//
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