H2136_AKKM8
ID H2136_AKKM8 Reviewed; 756 AA.
AC B2UPR7;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Beta-hexosaminidase Amuc_2136 {ECO:0000305};
DE EC=3.2.1.52 {ECO:0000269|PubMed:31345574};
DE AltName: Full=Beta-N-acetylhexosaminidase Am2136 {ECO:0000303|PubMed:31345574};
DE Flags: Precursor;
GN OrderedLocusNames=Amuc_2136 {ECO:0000312|EMBL:ACD05945.1};
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;
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 {ECO:0000312|Proteomes:UP000001031};
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:6JQF}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 23-756 IN COMPLEX WITH
RP N-ACETYLGLUCOSAMINE; CHLORIDE AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP ACTIVE SITES, AND MUTAGENESIS OF ASP-412 AND GLU-413.
RX PubMed=31345574; DOI=10.1016/j.bbrc.2019.06.150;
RA Chen X., Li M., Wang Y., Tang R., Zhang M.;
RT "Biochemical characteristics and crystallographic evidence for substrate-
RT assisted catalysis of a beta-N-acetylhexosaminidase in Akkermansia
RT muciniphila.";
RL Biochem. Biophys. Res. Commun. 517:29-35(2019).
CC -!- FUNCTION: Potentially capable of cleaving the specific glycoside
CC linkages in the process of mucin degradation in human intestinal tract
CC (Probable). Hydrolyzes synthetic substrate pNP-beta-GlcNAc with high
CC activity and pNP-beta-GalNAc to a lot lesser extent. Does not hydrolyze
CC pNP-alpha-GalNAc. {ECO:0000269|PubMed:31345574, 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:31345574};
CC -!- ACTIVITY REGULATION: Inhibited by Mn(2+) and Ca(2+) ions. Maintains 17%
CC and 60% of its enzymatic activity with Mn(2+) and Ca(2+), respectively.
CC No significant change in activity by the addition of Na(+), K(+) and
CC Mg(2+) ions. {ECO:0000269|PubMed:31345574}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.028 mM for pNP-beta-GlcNAc (at pH 8.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:31345574};
CC Vmax=394.47 umol/min/mg enzyme with pNP-beta-GlcNAc as substrate (at
CC pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:31345574};
CC Vmax=4.13 umol/min/mg enzyme with pNP-beta-GalNAc as substrate (at pH
CC 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:31345574};
CC Note=kcat is 5.57 sec(-1) and kcat/KM is 202.45 mM(-1)sec(-1) with
CC pNP-beta-GlcNAc as substrate. {ECO:0000269|PubMed:31345574};
CC pH dependence:
CC Stable enzymatic activity between pH 7.0 and pH 9.0. Significant
CC decrease in activity with pH lower than 7 and pH greater than 9.0.
CC {ECO:0000269|PubMed:31345574};
CC Temperature dependence:
CC Highest enzymatic activity at temperatures between 30 and 40 degrees
CC Celsius. Activity is decreased greatly above 45 or below 25 degrees
CC Celsius. {ECO:0000269|PubMed:31345574};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR EMBL; CP001071; ACD05945.1; -; Genomic_DNA.
DR RefSeq; WP_012421159.1; NC_010655.1.
DR PDB; 6JQF; X-ray; 1.90 A; A=23-756.
DR PDBsum; 6JQF; -.
DR AlphaFoldDB; B2UPR7; -.
DR SMR; B2UPR7; -.
DR STRING; 349741.Amuc_2136; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR EnsemblBacteria; ACD05945; ACD05945; Amuc_2136.
DR KEGG; amu:Amuc_2136; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_010969_2_0_0; -.
DR OMA; YWTGKEI; -.
DR OrthoDB; 727559at2; -.
DR BioCyc; AMUC349741:G1GBX-2279-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 Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..756
FT /note="Beta-hexosaminidase Amuc_2136"
FT /evidence="ECO:0000255"
FT /id="PRO_5002781815"
FT REGION 588..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:31345574,
FT ECO:0007744|PDB:6JQF"
FT ACT_SITE 344
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:31345574,
FT ECO:0007744|PDB:6JQF"
FT ACT_SITE 413
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:31345574,
FT ECO:0007744|PDB:6JQF"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31345574,
FT ECO:0007744|PDB:6JQF"
FT BINDING 412..413
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31345574,
FT ECO:0007744|PDB:6JQF"
FT BINDING 464
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31345574,
FT ECO:0007744|PDB:6JQF"
FT BINDING 490
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31345574,
FT ECO:0007744|PDB:6JQF"
FT BINDING 536..538
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31345574,
FT ECO:0007744|PDB:6JQF"
FT MUTAGEN 412
FT /note="D->A: No significant change in KM value, but 4297-
FT fold decrease in kcat/KM value compared to that of wild-
FT type."
FT /evidence="ECO:0000269|PubMed:31345574"
FT MUTAGEN 413
FT /note="E->A: No significant change in KM value, but 210-
FT fold decrease in kcat/KM value compared to that of wild-
FT type."
FT /evidence="ECO:0000269|PubMed:31345574"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:6JQF"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6JQF"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 200..216
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 334..344
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 376..390
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:6JQF"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:6JQF"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 418..434
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:6JQF"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:6JQF"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 471..476
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 504..510
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 528..535
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 549..568
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 577..587
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 610..615
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 623..633
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 642..647
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 650..655
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 662..665
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 681..690
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 693..698
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 701..705
FT /evidence="ECO:0007829|PDB:6JQF"
FT HELIX 712..714
FT /evidence="ECO:0007829|PDB:6JQF"
FT TURN 715..717
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:6JQF"
FT STRAND 746..755
FT /evidence="ECO:0007829|PDB:6JQF"
SQ SEQUENCE 756 AA; 83779 MW; 26226C47F23026D4 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 ARDLFYTKKE FADLVSYARK YGVNIVPEFD TPGHALSFTR LRPDLIYKGP
MNHEKRRCEM LDAANPETID LVSKVFDEYM LKDPKLGRPV FADCGVVHVG ADEFYGDKED
YRHFANAVLT HALKRGYTPR IWGSLSAKPG KTPVVSKGVQ MNLWSTGWMK AWEAVNQGYD
VINTNDGALY IVPFAGYYRM DRNHKGLYNN WIPNRIGNET LPSGHPQLLG GTFAVWNDET
DIMHTGYAPY DIWGIISGSM DVLSQKLWGT AKAPDTFEQH RELVSSIGNA PRTNPLHKWK
DSQPLTVKPS SLPQKLDKPA LGPNYRLTME LELTAAPEGK EQVLLAAPEG ELLAVMKDGT
VGFRRDDSLE FSFGAKLPVG KKVKVEIVGE PEKTSLLLDG EPAGTAVLKN FSDKSKDFSD
KFKHRPKVHR STFILPLKEL GSSFQGKVFH MNVQPL
