SGBU_HAEIN
ID SGBU_HAEIN Reviewed; 286 AA.
AC P44990;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative L-ribulose-5-phosphate 3-epimerase SgbU;
DE EC=5.1.3.22;
DE AltName: Full=L-xylulose-5-phosphate 3-epimerase;
GN Name=sgbU; OrderedLocusNames=HI_1026;
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 isomerization of L-xylulose-5-phosphate to L-
CC ribulose-5-phosphate. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ribulose 5-phosphate = L-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:18497, ChEBI:CHEBI:57829, ChEBI:CHEBI:58226;
CC EC=5.1.3.22;
CC -!- MISCELLANEOUS: Probably part of a sugar metabolic pathway along with
CC SgbH.
CC -!- SIMILARITY: Belongs to the L-ribulose-5-phosphate 3-epimerase family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22686.1; -; Genomic_DNA.
DR PIR; G64164; G64164.
DR RefSeq; NP_439186.1; NC_000907.1.
DR RefSeq; WP_005693360.1; NC_000907.1.
DR AlphaFoldDB; P44990; -.
DR SMR; P44990; -.
DR STRING; 71421.HI_1026; -.
DR DNASU; 950012; -.
DR EnsemblBacteria; AAC22686; AAC22686; HI_1026.
DR KEGG; hin:HI_1026; -.
DR PATRIC; fig|71421.8.peg.1070; -.
DR eggNOG; COG3623; Bacteria.
DR HOGENOM; CLU_082738_0_0_6; -.
DR OMA; CKGQFRD; -.
DR PhylomeDB; P44990; -.
DR BioCyc; HINF71421:G1GJ1-1066-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:InterPro.
DR GO; GO:0034015; F:L-ribulose-5-phosphate 3-epimerase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IBA:GO_Central.
DR CDD; cd00019; AP2Ec; 1.
DR InterPro; IPR001719; AP_endonuc_2.
DR InterPro; IPR004560; L-Ru-5P_3-Epase.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR00542; hxl6Piso_put; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome.
FT CHAIN 1..286
FT /note="Putative L-ribulose-5-phosphate 3-epimerase SgbU"
FT /id="PRO_0000097719"
SQ SEQUENCE 286 AA; 33062 MW; 689543EBBD5E89BB CRC64;
MKKHKIGIYE KALPKNITWQ ERLSLAKACG FEFIEMSIDE SNDRLSRLNW TKSERIALHQ
SIIQSGITIP SMCLSAHRRF PFGSKDKKIR QKSFEIMEKA IDLSVNLGIR TIQLAGYDVY
YEKQDEETIK YFQEGIEFAV TLAASAQVTL AVEIMDTPFM SSISRWKKWD TIINSPWFTV
YPDIGNLSAW NNNIEEELTL GIDKISAIHL KDTYPVTETS KGQFRDVPFG QGCVDFVHFF
SLLKKLNYRG AFLIEMWTEK NEEPLLEIIQ ARKWIVQQME KAGLLC
