ID B8H9Z5_PSECP Unreviewed; 231 AA.
AC B8H9Z5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=Achl_0380 {ECO:0000313|EMBL:ACL38379.1};
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL38379.1, ECO:0000313|Proteomes:UP000002505};
RN [1] {ECO:0000313|EMBL:ACL38379.1, ECO:0000313|Proteomes:UP000002505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 /
RC NCIMB 13794 / A6 {ECO:0000313|Proteomes:UP000002505};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) 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; CP001341; ACL38379.1; -; Genomic_DNA.
DR RefSeq; WP_015935606.1; NC_011886.1.
DR AlphaFoldDB; B8H9Z5; -.
DR STRING; 452863.Achl_0380; -.
DR KEGG; ach:Achl_0380; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_3_0_11; -.
DR OrthoDB; 9786287at2; -.
DR Proteomes; UP000002505; Chromosome.
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;
FT DOMAIN 14..202
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 231 AA; 24329 MW; DBF76D61B75803EC CRC64;
MSAALLEAIA LTRADVCALH AELTRYGLVV WTAGNVSARV PGTDLMVIKP SGVSYQDLAP
DQMVVTDLYG TPVSGNGEGG WGNPALSPSS DTAAHAYVYR HMPEVGGVVH THSTYATAWA
ARGEAIPCVL TMMSDEFGGE IPVGPFALIG DDSIGHGIVE TLKNSNSPAV LMQNHGPFTI
GKDAKSAVKA AVMCEEVART VHVARQLGDP LPIDQGHIDS LYARYQNVYG Q
//
