FRLB_BACSU
ID FRLB_BACSU Reviewed; 328 AA.
AC O32157;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Fructosamine deglycase FrlB;
DE EC=3.5.-.-;
GN Name=frlB; Synonyms=yurP; OrderedLocusNames=BSU32610;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15556630; DOI=10.1016/j.febslet.2004.10.049;
RA Wiame E., Duquenne A., Delpierre G., Van Schaftingen E.;
RT "Identification of enzymes acting on alpha-glycated amino acids in Bacillus
RT subtilis.";
RL FEBS Lett. 577:469-472(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of yurP protein (np_391141.1) from Bacillus subtilis at
RT 1.90 a resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of a range of fructosamine 6-
CC phosphates to glucose 6-phosphate and a free amino acid.
CC {ECO:0000269|PubMed:15556630}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 mM for fructosevaline-6-phosphate (at 30 degrees Celsius and
CC pH 7.1) {ECO:0000269|PubMed:15556630};
CC KM=0.16 mM for fructoseglycine-6-phosphate (at 30 degrees Celsius and
CC pH 7.1) {ECO:0000269|PubMed:15556630};
CC KM=1.2 mM for fructoselysine-6-phosphate (at 30 degrees Celsius and
CC pH 7.1) {ECO:0000269|PubMed:15556630};
CC Vmax=0.01 umol/min/mg enzyme with fructoselysine-6-phosphate as
CC substrate (at 30 degrees Celsius and pH 7.1)
CC {ECO:0000269|PubMed:15556630};
CC Vmax=0.1 umol/min/mg enzyme with fructoseglycine-6-phosphate as
CC substrate (at 30 degrees Celsius and pH 7.1)
CC {ECO:0000269|PubMed:15556630};
CC Vmax=0.5 umol/min/mg enzyme with fructosevaline-6-phosphate as
CC substrate (at 30 degrees Celsius and pH 7.1)
CC {ECO:0000269|PubMed:15556630};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|Ref.3}.
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DR EMBL; AL009126; CAB15251.1; -; Genomic_DNA.
DR PIR; G70018; G70018.
DR RefSeq; NP_391141.1; NC_000964.3.
DR RefSeq; WP_003243688.1; NZ_JNCM01000033.1.
DR PDB; 3EUA; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-328.
DR PDBsum; 3EUA; -.
DR AlphaFoldDB; O32157; -.
DR SMR; O32157; -.
DR STRING; 224308.BSU32610; -.
DR PaxDb; O32157; -.
DR PRIDE; O32157; -.
DR EnsemblBacteria; CAB15251; CAB15251; BSU_32610.
DR GeneID; 936701; -.
DR KEGG; bsu:BSU32610; -.
DR PATRIC; fig|224308.179.peg.3531; -.
DR eggNOG; COG2222; Bacteria.
DR InParanoid; O32157; -.
DR OMA; LMEMQWI; -.
DR PhylomeDB; O32157; -.
DR BioCyc; BSUB:BSU32610-MON; -.
DR SABIO-RK; O32157; -.
DR EvolutionaryTrace; O32157; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd05710; SIS_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR InterPro; IPR035488; FrlB_SIS.
DR InterPro; IPR024713; Fructosamine_deglycase_FrlB.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF009290; FrlB; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Hydrolase; Reference proteome;
KW Repeat.
FT CHAIN 1..328
FT /note="Fructosamine deglycase FrlB"
FT /id="PRO_0000387992"
FT DOMAIN 15..153
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 181..311
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:3EUA"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:3EUA"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:3EUA"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:3EUA"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:3EUA"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 157..189
FT /evidence="ECO:0007829|PDB:3EUA"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:3EUA"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:3EUA"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:3EUA"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:3EUA"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:3EUA"
FT HELIX 287..312
FT /evidence="ECO:0007829|PDB:3EUA"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:3EUA"
SQ SEQUENCE 328 AA; 36876 MW; 598C0214F1C4B98C CRC64;
MSQATAKVNR EVQAFLQDLK GKTIDHVFFV ACGGSSAIMY PSKYVFDRES KSINSDLYSA
NEFIQRNPVQ LGEKSLVILC SHSGNTPETV KAAAFARGKG ALTIAMTFKP ESPLAQEAQY
VAQYDWGDEA LAINTNYGVL YQIVFGTLQV LENNTKFEQA IEGLDQLQAV YEKALKQEAD
NAKQFAKAHE KESIIYTMAS GANYGVAYSY SICILMEMQW IHSHAIHAGE YFHGPFEIID
ESVPFIILLG LDETRPLEER ALTFSKKYGK KLTVLDAASY DFTAIDDSVK GYLAPLVLNR
VLRSYADELA EERNHPLSHR RYMWKVEY
