ID A0A160KW44_9MICO Unreviewed; 236 AA.
AC A0A160KW44;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-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=A6122_2523 {ECO:0000313|EMBL:AND17638.1}, C5C18_13990
GN {ECO:0000313|EMBL:PPG04090.1};
OS Rathayibacter tritici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=33888 {ECO:0000313|EMBL:AND17638.1, ECO:0000313|Proteomes:UP000077071};
RN [1] {ECO:0000313|EMBL:AND17638.1, ECO:0000313|Proteomes:UP000077071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND17638.1,
RC ECO:0000313|Proteomes:UP000077071};
RA Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PPG04090.1, ECO:0000313|Proteomes:UP000239776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSPB 2748 {ECO:0000313|EMBL:PPG04090.1,
RC ECO:0000313|Proteomes:UP000239776};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) 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; CP015515; AND17638.1; -; Genomic_DNA.
DR EMBL; PSUO01000035; PPG04090.1; -; Genomic_DNA.
DR RefSeq; WP_068255762.1; NZ_PSWT01000005.1.
DR AlphaFoldDB; A0A160KW44; -.
DR STRING; 33888.A6122_2523; -.
DR KEGG; rtn:A6122_2523; -.
DR PATRIC; fig|33888.3.peg.2822; -.
DR OrthoDB; 9786287at2; -.
DR Proteomes; UP000077071; Chromosome.
DR Proteomes; UP000239776; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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 Reference proteome {ECO:0000313|Proteomes:UP000077071}.
FT DOMAIN 17..200
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 236 AA; 24832 MW; AF4B133B287A7B30 CRC64;
MTTLTPAVEE AIARVREDVA RLHAELVRYG LVIWTGGNIS GRVPGADLFV IKPSGVSYDD
LAPSNMILCD LDGAVVPGTP GSDRSPSSDT AAHAYVYREM PEVGGVVHTH STYATAWAAR
AEPIPCVITA MADEFGGDIP VGPFAIIGDD SIGRGIVSTL AGHRSRAVLM QNHGVFTIGK
DAKDAVKAAV MAEDVARTVH LARQGGDLVP LPQESIDALF DRYQNVYGQN PTGAIA
//
