ID   SGBE_HAEIN              Reviewed;         231 AA.
AC   P44989;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=L-ribulose-5-phosphate 4-epimerase SgbE {ECO:0000250|UniProtKB:P37680};
DE            EC=5.1.3.4 {ECO:0000250|UniProtKB:P37680};
DE   AltName: Full=Phosphoribulose isomerase {ECO:0000250|UniProtKB:P37680};
GN   Name=sgbE {ECO:0000250|UniProtKB:P37680}; OrderedLocusNames=HI_1025;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Catalyzes the interconversion of L-ribulose 5-phosphate
CC       (LRu5P) and D-xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol
CC       mechanism (carbon-carbon bond cleavage analogous to a class II aldolase
CC       reaction). May be involved in the utilization of 2,3-diketo-L-gulonate.
CC       {ECO:0000250|UniProtKB:P37680}.
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:0000250|UniProtKB:P37680};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P08203};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08203};
CC   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC       subfamily. {ECO:0000250|UniProtKB:P37680}.
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DR   EMBL; L42023; AAC22685.1; -; Genomic_DNA.
DR   RefSeq; NP_439185.1; NC_000907.1.
DR   RefSeq; WP_005669745.1; NC_000907.1.
DR   AlphaFoldDB; P44989; -.
DR   SMR; P44989; -.
DR   STRING; 71421.HI_1025; -.
DR   EnsemblBacteria; AAC22685; AAC22685; HI_1025.
DR   KEGG; hin:HI_1025; -.
DR   PATRIC; fig|71421.8.peg.1069; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_006033_5_0_6; -.
DR   OMA; AHERYMT; -.
DR   PhylomeDB; P44989; -.
DR   BioCyc; HINF71421:G1GJ1-1065-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central.
DR   GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0019572; P:L-arabinose catabolic process; IEA:InterPro.
DR   GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.225.10; -; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   InterPro; IPR004661; AraD.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; SSF53639; 1.
DR   TIGRFAMs; TIGR00760; araD; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Metal-binding; Reference proteome;
KW   Zinc.
FT   CHAIN           1..231
FT                   /note="L-ribulose-5-phosphate 4-epimerase SgbE"
FT                   /id="PRO_0000162924"
FT   ACT_SITE        120
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
FT   ACT_SITE        229
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
FT   BINDING         27..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         44..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         74..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
SQ   SEQUENCE   231 AA;  25981 MW;  9DE3485E54B10DC7 CRC64;
     MLAQLKKEVF EANLALPKHH LVTFTWGNVS AIDREKNLVV IKPSGVDYDV MTENDMVVVD
     LFTGNIVEGN KKPSSDTPTH LELYRQFPHI GGIVHTHSRH ATIWAQAGLD IIEVGTTHGD
     YFYGTIPCTR QMTTKEIKGN YELETGKVIV ETFLSRGIEP DNIPAVLVHS HGPFAWGKDA
     NNAVHNAVVL EEVAYMNLFS QQLNPYLSPM QKDLLDKHYL RKHGQNAYYG Q