ID R6WVI9_9FIRM Unreviewed; 233 AA.
AC R6WVI9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=BN605_01425 {ECO:0000313|EMBL:CDD08031.1};
OS Dorea sp. CAG:317.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=1262873 {ECO:0000313|EMBL:CDD08031.1, ECO:0000313|Proteomes:UP000018262};
RN [1] {ECO:0000313|EMBL:CDD08031.1, ECO:0000313|Proteomes:UP000018262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:317 {ECO:0000313|Proteomes:UP000018262};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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}.
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:CDD08031.1}.
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DR EMBL; CBGJ010000088; CDD08031.1; -; Genomic_DNA.
DR AlphaFoldDB; R6WVI9; -.
DR STRING; 1262873.BN605_01425; -.
DR Proteomes; UP000018262; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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 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:UP000018262}.
FT DOMAIN 7..197
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 233 AA; 26033 MW; 7D59F2B0E1285762 CRC64;
MLEQLKKEVY EANMLLPKYD LVTFTWGNVS GIDREKGLFV IKPSGVEYDK LTPEDMVVVD
LDGNKVEGKY NPSSDTATHV ELYNRFPQIG GVVHTHSPWA TSWAQAGRGI PCYGTTHADY
LYGEVPCVRN LTKEEIDEAY EKNTGVLIVD HFEACGIDSE AMPAVLCKNH GPFTWGKDAN
EAVHNAVVLE EVAKMAARCE MINPKNQPAP QELQDKHYYR KHGANAYYGQ PGK
//
