ID A0A2A2EFU9_9BIFI Unreviewed; 230 AA.
AC A0A2A2EFU9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=B1526_0842 {ECO:0000313|EMBL:PAU67867.1};
OS Bifidobacterium criceti.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1960969 {ECO:0000313|EMBL:PAU67867.1, ECO:0000313|Proteomes:UP000218399};
RN [1] {ECO:0000313|EMBL:PAU67867.1, ECO:0000313|Proteomes:UP000218399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=71 {ECO:0000313|EMBL:PAU67867.1,
RC ECO:0000313|Proteomes:UP000218399};
RX PubMed=28837128; DOI=10.1038/ismej.2017.138;
RA Milani C., Mangifesta M., Mancabelli L., Lugli G.A., James K., Duranti S.,
RA Turroni F., Ferrario C., Ossiprandi M.C., van Sinderen D., Ventura M.;
RT "Unveiling bifidobacterial biogeography across the mammalian branch of the
RT tree of life.";
RL ISME J. 11:2834-2847(2017).
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:PAU67867.1}.
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DR EMBL; MVOH01000008; PAU67867.1; -; Genomic_DNA.
DR RefSeq; WP_022857911.1; NZ_MVOH01000008.1.
DR AlphaFoldDB; A0A2A2EFU9; -.
DR GeneID; 61075019; -.
DR OrthoDB; 9786287at2; -.
DR Proteomes; UP000218399; 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;
FT DOMAIN 20..200
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 230 AA; 25112 MW; E27E4B1100155E9A CRC64;
MATLAEYGPE VRAEVKQVRE VVASLHEQLI KWNLVVWTAG NVSQRLRTAD LMVIKPSGLR
YEYLTPSSMV VCDLDGNVVD GAESPSSDTA SHAYIYRHMP DVYGVVHTHS TYATAWAATG
QNIPCGLTMM GDEFGGDVPV GPFRLIGSEA IGEGVVETLK QYPKSPAVLM QNHGPFTIGK
DAEAAVKAAA MTEEVAHTMW AARQLGEIIP IPQEDIDKLN DRYQNVYGQH
//
