ID A2RKF2_LACLM Unreviewed; 664 AA. AC A2RKF2; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 04-NOV-2026, entry version 88. DE SubName: Full=AguA protein {ECO:0000313|EMBL:CAL97762.1}; DE EC=3.2.1.139 {ECO:0000313|EMBL:CAL97762.1}; GN Name=aguA {ECO:0000313|EMBL:CAL97762.1}; GN OrderedLocusNames=llmg_1169 {ECO:0000313|EMBL:CAL97762.1}; OS Lactococcus lactis subsp. cremoris (strain MG1363). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus; Lactococcus cremoris subsp. cremoris. OX NCBI_TaxID=416870 {ECO:0000313|EMBL:CAL97762.1, ECO:0000313|Proteomes:UP000000364}; RN [1] {ECO:0000313|EMBL:CAL97762.1, ECO:0000313|Proteomes:UP000000364} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MG1363 {ECO:0000313|EMBL:CAL97762.1, RC ECO:0000313|Proteomes:UP000000364}; RX PubMed=17307855; DOI=10.1128/JB.01768-06; RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., RA van Sinderen D., Kok J.; RT "The complete genome sequence of the lactic acid bacterial paradigm RT Lactococcus lactis subsp. cremoris MG1363."; RL J. Bacteriol. 189:3256-3270(2007). 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; AM406671; CAL97762.1; -; Genomic_DNA. DR RefSeq; WP_011835070.1; NC_009004.1. DR AlphaFoldDB; A2RKF2; -. DR SMR; A2RKF2; -. DR STRING; 416870.llmg_1169; -. DR PaxDb; 416870-llmg_1169; -. DR KEGG; llm:llmg_1169; -. DR eggNOG; COG3661; Bacteria. DR HOGENOM; CLU_007125_1_0_9; -. DR OMA; AAIFRNW; -. DR OrthoDB; 339499at2; -. DR Proteomes; UP000000364; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0046559; F:alpha-glucuronidase activity; IEA:UniProtKB-EC. DR GO; GO:0033939; F:xylan alpha-1,2-glucuronosidase activity; IEA:TreeGrafter. DR GO; GO:0045493; P:xylan catabolic process; IEA:InterPro. DR Gene3D; 3.90.1330.10; Alpha-glucuronidase, C-terminal domain; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR037054; A-glucoronidase_C_sf. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR011099; Glyco_hydro_67_C. DR InterPro; IPR011100; Glyco_hydro_67_cat. DR PANTHER; PTHR39207; ALPHA-GLUCURONIDASE A; 1. DR PANTHER; PTHR39207:SF1; ALPHA-GLUCURONIDASE A; 1. DR Pfam; PF07477; Glyco_hydro_67C; 1. DR Pfam; PF07488; Glyco_hydro_67M; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 4: Predicted; KW Glycosidase {ECO:0000313|EMBL:CAL97762.1}; KW Hydrolase {ECO:0000313|EMBL:CAL97762.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000364}. FT DOMAIN 103..436 FT /note="Glycosyl hydrolase family 67 catalytic" FT /evidence="ECO:0000259|Pfam:PF07488" FT DOMAIN 437..660 FT /note="Glycosyl hydrolase family 67 C-terminal" FT /evidence="ECO:0000259|Pfam:PF07477" SQ SEQUENCE 664 AA; 75975 MW; 1F2144C6C7866DCD CRC64; MAIDEMWLQF SILKKRLTNE IFYVNLEYED KITIRLRSEI CEWLGCQLTG EKSEATVVLS VNSKLDDNLE AYEVKENEII GASSVGLLYG FYAYLRLKLS GANLSEKSAP AQSLRMINHW DQVDGTIERG YAGESIFFGR FGSNDNTDTG SFAVKNIGTD IFRNDFTRLK MYARFLASIG INAISLNNVN VRGLGTSLIV SPYIEKVGEI SKLFATFGLK TFLAINWAAP KLIGELKTSD PLDENVYTWW QQTIDHIYEV IPDFGGFVVK ADSEGEPGPY QYGRNHADGA NMLAKAFEKY NGLVIWRTFV YNSQTDWRKR KNDRAKAAYE NFMPLDGDFS DNVILQIKFG PIDFGVREPL MPLFGALKKT NQLMEFQITA EYLGHQLDLN YVLPQWLEMI HFDNYGQPKD TIRANSPVAT HSGFIAIGNV GMDENWCGNK LSQANFYGFG RMCWNNDLTA TEILQEWIAL TFSEVKAEVQ KEIFELLIDS NQTYELYNAP LAVGSMMVPH YHYGPSINGY EYDRWGAYHF SDRNGLGIDR TTATGTGFAS LYAPEVAKVF EDKSKTPDEI LLFFHYVEYG HLLHNGKTLI QTIYDQHFEG FERVKSYIKS WKSLKGQVDE ATYDNVADRL ERQLEHARNW RDQVNTYFYR MSGIPDDQGR EIYR //