H0868_AKKM8
ID H0868_AKKM8 Reviewed; 549 AA.
AC B2UQG6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Beta-hexosaminidase Amuc_0868 {ECO:0000305};
DE EC=3.2.1.52 {ECO:0000269|PubMed:32819592};
DE AltName: Full=Beta-N-acetylhexosaminidase Am0868 {ECO:0000303|PubMed:32819592};
DE Flags: Precursor;
GN OrderedLocusNames=Amuc_0868 {ECO:0000312|EMBL:ACD04701.1};
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741 {ECO:0000312|EMBL:ACD04701.1};
RN [1] {ECO:0000312|Proteomes:UP000001031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC 107961 / Muc;
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
RN [2] {ECO:0007744|PDB:7CBN, ECO:0007744|PDB:7CBO}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 29-549 AND IN COMPLEX WITH
RP N-ACETYLGLUCOSAMINE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITES, AND
RP MUTAGENESIS OF ASP-326 AND GLU-327.
RX PubMed=32819592; DOI=10.1016/j.bbrc.2020.06.116;
RA Xu W., Yang W., Wang Y., Wang M., Zhang M.;
RT "Structural and biochemical analyses of beta-N-acetylhexosaminidase Am0868
RT from Akkermansia muciniphila involved in mucin degradation.";
RL Biochem. Biophys. Res. Commun. 529:876-881(2020).
CC -!- FUNCTION: Potentially capable of cleaving the specific glycoside
CC linkages in the process of mucin degradation in human intestinal tract
CC (Probable). Hydrolyzes chromogenic substrates pNP-beta-GlcNAc with high
CC activity and pNP-beta-GalNAc to a lesser extent, but not pNP-beta-
CC glucose or pNP-beta-galactose (PubMed:32819592).
CC {ECO:0000269|PubMed:32819592, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000269|PubMed:32819592};
CC -!- ACTIVITY REGULATION: Inhibited strongly by Cu(2+), Zn(2+), Cd(2+) and
CC Ni(2+) ions. No effect on activity with Na(+), Li(+), K(+), Ca(2+),
CC Mg(2+) or Mn(2+) ions. {ECO:0000269|PubMed:32819592}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.297 mM for pNP-GlcNAc (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:32819592};
CC Vmax=86.3 mmol/min/mg enzyme with pNP-GlcNAc as substrate (at pH 7.0
CC and 37 degrees Celsius) {ECO:0000269|PubMed:32819592};
CC Note=kcat is 51.39 sec(-1) and kcat/KM is 1.73 M(-1)sec(-1) with pNP-
CC GlcNAc as substrate. {ECO:0000269|PubMed:32819592};
CC pH dependence:
CC Optimum pH is approximately 7. Stable activity from pH 4.5 to 8.5.
CC Retains more than 30% of activity at pH 9.0.
CC {ECO:0000269|PubMed:32819592};
CC Temperature dependence:
CC Highest activity at 45 degrees Celsius. Has about 40% of activity at
CC 55 degrees Celsius. {ECO:0000269|PubMed:32819592};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR EMBL; CP001071; ACD04701.1; -; Genomic_DNA.
DR RefSeq; WP_012419916.1; NC_010655.1.
DR PDB; 7CBN; X-ray; 1.70 A; A=29-549.
DR PDB; 7CBO; X-ray; 1.50 A; A=29-549.
DR PDBsum; 7CBN; -.
DR PDBsum; 7CBO; -.
DR AlphaFoldDB; B2UQG6; -.
DR SMR; B2UQG6; -.
DR STRING; 349741.Amuc_0868; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR EnsemblBacteria; ACD04701; ACD04701; Amuc_0868.
DR KEGG; amu:Amuc_0868; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_007082_5_1_0; -.
DR OMA; GHDVVMC; -.
DR OrthoDB; 727559at2; -.
DR BioCyc; AMUC349741:G1GBX-940-MON; -.
DR Proteomes; UP000001031; Chromosome.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.379.10; -; 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; PTHR22600; PTHR22600; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..549
FT /note="Beta-hexosaminidase Amuc_0868"
FT /evidence="ECO:0000255"
FT /id="PRO_5002783767"
FT REGION 526..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:32819592,
FT ECO:0007744|PDB:7CBO"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:32819592,
FT ECO:0007744|PDB:7CBO"
FT ACT_SITE 327
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:32819592,
FT ECO:0007744|PDB:7CBO"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:32819592,
FT ECO:0007744|PDB:7CBO"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:32819592,
FT ECO:0007744|PDB:7CBO"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:32819592,
FT ECO:0007744|PDB:7CBO"
FT BINDING 420..422
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:32819592,
FT ECO:0007744|PDB:7CBO"
FT BINDING 474..476
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:32819592,
FT ECO:0007744|PDB:7CBO"
FT MUTAGEN 326
FT /note="D->A: Specific activity is decreased by 99% with a
FT 145-fold reduction in kcat/Km value compared to that of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:32819592"
FT MUTAGEN 327
FT /note="E->A: Specific activity is decreased by 86% with a
FT 10-fold reduction in kcat/Km value compared to that of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:32819592"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:7CBO"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:7CBO"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:7CBO"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:7CBO"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 250..260
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 298..314
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 351..368
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 399..406
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:7CBO"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 445..449
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 460..465
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 466..473
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 481..488
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 491..500
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:7CBO"
FT HELIX 508..524
FT /evidence="ECO:0007829|PDB:7CBO"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:7CBO"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:7CBO"
SQ SEQUENCE 549 AA; 61830 MW; D1FA1A39FFBBE09E CRC64;
MISKCTFSAT VFSLFSLCWG APSSPVLEAP HTIPLPAAMR VQTGESGFSL KNGVRLPEKN
PLSRQAERIF RDNGINTALV KNNADIIFTE DASLGREGYR LAVTPDSISI ASGSVNGTLY
ALQSLVQSIA ADKNGAPALP RMDVKDQPRF SWRGLMVDSC RHMMPVRDIK KVLDLMERYK
FNTLHWHLTD DQGWRLPIAK YPRLTTVGGA RAQSPVIGNR NKGDGIPYSG HYTADEIRDV
VRYARDRGIT VIPEVEMPGH ASAAIAAYPE LGNTDIPGYE PRVQETWGVH SYTFSPTEKT
FRFLEDVIDE ICALFPDSPY IHIGGDEAPK NQWKQSPTAQ RVMKDNGLAN EHELQSYFIR
RVEKMINNRG KRLIGWDEIQ EGGLSPTATM MVWRSQMPHI AAQALAQGND IVMTPNSHLY
FDYDQGPGKP AAPEYETINN NQLTWQHVYG LEPVPQGTPR EREKQVLGCQ ANIWTEYIPN
LPKWEYHVFP RALALAEVAW TPQELKNEKD FRKRLDRQLP FLDARGVNYK RPDNGAPAQP
KAVITRERR
