ID R5S8J4_9CLOT Unreviewed; 232 AA.
AC R5S8J4;
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=BN479_01464 {ECO:0000313|EMBL:CCZ41407.1};
OS Clostridium sp. CAG:122.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262773 {ECO:0000313|EMBL:CCZ41407.1, ECO:0000313|Proteomes:UP000017991};
RN [1] {ECO:0000313|EMBL:CCZ41407.1, ECO:0000313|Proteomes:UP000017991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:122 {ECO:0000313|Proteomes:UP000017991};
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:CCZ41407.1}.
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DR EMBL; CAZY010000109; CCZ41407.1; -; Genomic_DNA.
DR AlphaFoldDB; R5S8J4; -.
DR Proteomes; UP000017991; 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:UP000017991}.
FT DOMAIN 7..197
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 232 AA; 25914 MW; 08A88483AB630EFE CRC64;
MLEELKKRVY EANMLLPKYG LVTFTWGNVS EIDRESGIFA IKPSGVEYDK LTPEDMVLVD
LNGNKVEGKY NPSSDTATHV ELYKAFKDIG GVVHTHSSYA TSWAQAGRSI PCYGTTHADY
IYGEVPCVRC LTKDEIEDAY EENTGKLIVS EFNARNLDPV AVPAVLCKNH GPFAWGKDAH
EAVHNAVVLE EVGKMAYRAE TINPRIQPAP QELQDKHYYR KHGANAYYGQ GK
//
