ID B3DP83_BIFLD Unreviewed; 606 AA. AC B3DP83; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 75. DE SubName: Full=Glycosidase {ECO:0000313|EMBL:ACD98942.1}; GN OrderedLocusNames=BLD_1497 {ECO:0000313|EMBL:ACD98942.1}; OS Bifidobacterium longum (strain DJO10A). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=205913 {ECO:0000313|EMBL:ACD98942.1, ECO:0000313|Proteomes:UP000002419}; RN [1] {ECO:0000313|EMBL:ACD98942.1, ECO:0000313|Proteomes:UP000002419} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJO10A {ECO:0000313|EMBL:ACD98942.1, RC ECO:0000313|Proteomes:UP000002419}; RX PubMed=16391088; DOI=10.1128/AEM.72.1.527-535.2006; RA Lee J.H., O'Sullivan D.J.; RT "Sequence analysis of two cryptic plasmids from Bifidobacterium longum RT DJO10A and construction of a shuttle cloning vector."; RL Appl. Environ. Microbiol. 72:527-535(2006). RN [2] {ECO:0000313|EMBL:ACD98942.1, ECO:0000313|Proteomes:UP000002419} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJO10A {ECO:0000313|EMBL:ACD98942.1, RC ECO:0000313|Proteomes:UP000002419}; RX PubMed=18505588; DOI=10.1186/1471-2164-9-247; RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., RA Slesarev A.I., Weimer B., O'Sullivan D.J.; RT "Comparative genomic analysis of the gut bacterium Bifidobacterium longum RT reveals loci susceptible to deletion during pure culture growth."; RL BMC Genomics 9:247-247(2008). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000605; ACD98942.1; -; Genomic_DNA. DR RefSeq; WP_007057515.1; NZ_AABM02000008.1. DR AlphaFoldDB; B3DP83; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; blj:BLD_1497; -. DR HOGENOM; CLU_006462_1_2_11; -. DR Proteomes; UP000002419; Chromosome. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR022567; DUF3459. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR045857; O16G_dom_2. DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1. DR PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF11941; DUF3459; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 4: Predicted; KW Glycosidase {ECO:0000313|EMBL:ACD98942.1}; KW Hydrolase {ECO:0000313|EMBL:ACD98942.1}. FT DOMAIN 31..458 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" SQ SEQUENCE 606 AA; 68126 MW; ADBE648C1DCE2534 CRC64; MTTFNRAIIP DAIRTNGATP NPWWSNAVVY QIYPRSFQDT NGDGFGDLKG ITSRLDYLAD LGVDVLWLSP VYKSPQDDNG YDISDYQDID PLFGTLDDMD ELLAEAHKRG LKIVMDLVVN HTSDEHAWFE ASKNKDDEHA DWYWWRPARP GTTPGEPGAE PNQWGSYFGG SAWEYCPERG EYFLHQFSKK QPDLNWENPA VRRAVYDMMN WWLDRGVDGF RMDVITLISK RTDSNGKLPG EYGSELEDLP VGEEGYSNPN PFCADGPRQD EFLAEMRREV FEGREGFLTV GEAPGVTAQR NEHITDPGNG ELDMLFLFEH VDFDCEGTKW KPLPLDLPKF KSIMAGYQTA VQNAGWASLF TGNHDQPRVV SRWGDDSAEE SRVRSAKALG LMLHMHRGTP YIYQGEELGM TDAHFTRLDQ YRDLESLNAY RQRVEEAKVQ SSESMMAGLA ARSRDNARTP MQWDGSGYAG FTAPDAATEP WISVNPNHAE INAAGEFDDP DSVYSFYKQL VALRHNSPVV AAGDWRLIDA ADPHVYAFTR ELDAEKLLVV VNMSSRTVDL PREAAELTAV GIAEPNVVIS TYDAPHTVAS LANRELDPWE AAVIQL //