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Database: UniProt
Entry: R6JD54_9BACT
LinkDB: R6JD54_9BACT
Original site: R6JD54_9BACT 
ID   R6JD54_9BACT            Unreviewed;       756 AA.
AC   R6JD54;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Glycoside hydrolase family 20 catalytic core {ECO:0000313|EMBL:CDB56544.1};
GN   ORFNames=BN502_00073 {ECO:0000313|EMBL:CDB56544.1};
OS   Akkermansia muciniphila CAG:154.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=1263034 {ECO:0000313|EMBL:CDB56544.1, ECO:0000313|Proteomes:UP000018106};
RN   [1] {ECO:0000313|EMBL:CDB56544.1, ECO:0000313|Proteomes:UP000018106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:154 {ECO:0000313|Proteomes:UP000018106};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDB56544.1}.
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DR   EMBL; CBDW010000161; CDB56544.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6JD54; -.
DR   Proteomes; UP000018106; Unassembled WGS sequence.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06564; GH20_DspB_LnbB-like; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR015882; HEX_bac_N.
DR   PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR   PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDB56544.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..756
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004410384"
FT   DOMAIN          110..228
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          232..414
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   REGION          588..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        413
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   756 AA;  83771 MW;  CBCC8396F55A6C54 CRC64;
     MKKNLFLMIA VLAASPVMGQ DAKQIADSLS IPPVKAGAKQ LPMPSVSGAQ IKLLGADYEQ
     LVNSKGKIAP VISDTPVNVS FKVTKDGKEA VSKDYEIMLQ APQAAQGNPK PRIIPEILQW
     KGGQGEYKLG NTVTIACPDK ELGKLFAADM EDVLGKKVKL VAPGAKADIS LSLLKGGNLG
     REGYRLQIAR DGVRLGAAAP TGLFWGTRTL LQMLRQTPGS VPCGTAVDFP RYQLRGFMLD
     VARTPYPLSY LKDVIRTMAW YKMNDLHLVI NNNYIFHEHY VDNGHDPFKE SYAAFRLESK
     MKGKDGTPLT AKDLFYTKKE FADLVSYARK YGVNIVPEFD TPGHALSFTR LRPDLIYKGP
     MNHEKRRCEM LDAANPETID LVSKVFDEYM LKDPKLGRPV FADCGVVHVG ADEFYGDKED
     YRHFANAVLS HALKRGYTPR IWGSLSAKPG KTPVVSKGVQ MNLWSTGWMK AWEAVNQGYD
     VINTNDGALY IVPFAGYYRM DRNHKGLYNN WIPNRIGNET LPSGHPQLLG GTFAVWNDET
     DIMHTGYAPY DIWGIISGSM DVLSQKLWGT AKAPDTFEQH RELVSSIGNA PRTNPLHKWK
     DSQPFTVKPS SLPQKLDKPA LGPNYRLTME LELTAAPEGK EQVLLAAPEG ELLAVMKDGT
     VGFRRDDSLE FSFGAKLPVG KKVKVEIVGE PEKTSLLLDG EPAGTAVLKN FSDKSKDFSD
     KFKHRPKVHR STFILPLKEL GSSFQGKVFH MNVQPL
//
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