ID J9FXM4_9ZZZZ Unreviewed; 757 AA.
AC J9FXM4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=EVA_12568 {ECO:0000313|EMBL:EJW99308.1};
OS gut metagenome.
OC unclassified sequences; metagenomes; organismal metagenomes.
OX NCBI_TaxID=749906 {ECO:0000313|EMBL:EJW99308.1};
RN [1] {ECO:0000313|EMBL:EJW99308.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23251564; DOI=10.1371/journal.pone.0051521;
RA Alcaide M., Messina E., Richter M., Bargiela R., Peplies J., Huws S.A.,
RA Newbold C.J., Golyshin P.N., Simon M.A., Lopez G., Yakimov M.M., Ferrer M.;
RT "Gene sets for utilization of primary and secondary nutrition supplies in
RT the distal gut of endangered iberian lynx.";
RL PLoS ONE 7:E51521-E51521(2012).
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:EJW99308.1}.
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DR EMBL; AMCI01003864; EJW99308.1; -; Genomic_DNA.
DR AlphaFoldDB; J9FXM4; -.
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; cd06563; GH20_chitobiase-like; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF13290; CHB_HEX_C_1; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 621..755
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 757 AA; 84614 MW; 33106F1328A86286 CRC64;
MASCLFAGAL LLGACTQTPP VTEEIALIPA PLQLEQTTGA FVVKSGTTIG VDDATLLPAG
EYLAQLLAPA TGYTLKVKEG KGDIQLTLGQ TLDKEGAYTL NADNSGVTIT GHDYAGVLAG
IATFRQLLPD AIESDEKVSG TDWAIPAVRI EDAPRYPWRG MMLDVSRHFY DVNEVKEFLD
VMALYKMNKF HWHLTDDQGW RVEIKKYPLL TEKGAWRKYN SHDRECLRQA KDNPDMAIPE
DKIRIVEGDT LYGGFYTQKD IQDVIAYAQV RGIDIIPEVD MPGHMLAAVS NYEGVSCFSE
TGWGSVFSSP VCPGKESALE FCKNVYSEII DLFPYKYVHI GGDEVEKTNW KKCPDCQKRM
RDQGLKTEEE LQSWFIHYME HFFNEKGKEM IGWDEIIEGG LSKTATVMWW RSWVKDAAAK
ATAQGNPVIF TPNGQFYLDY AEDINSIPSI YNLDLNEGMT PEQQALIQGV QGNIWCEWIP
SNDRMQYMSI PRLVAIAEKG WADDSQKDLE GFRERLSSQY NRLNVMGINY RIPDLEGFHA
VNAFIGEGDV KVTCLDPTAQ IRYTTDGSTP TLESPLYEGP VKVTETTDFT FCTFRPSGKR
GDIVKTRFIQ SEYAPAVKAA PSNPGLKATW HEFKGDRCAD IEKARVNGTY TIEDVVIPKK
VKGNIGLIIR GYFNAPKDDI YTFALLSDDG STLAIDGEQV IDNDRPHGPK EVIGQKAMAK
GYHPMEVRYF DQNGGQLKLK VTGSDGKEIP FTHLYAY
//
