ID R6AX72_9BACT Unreviewed; 775 AA.
AC R6AX72;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=BN693_00289 {ECO:0000313|EMBL:CDA45727.1};
OS Prevotella sp. CAG:5226.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262930 {ECO:0000313|EMBL:CDA45727.1, ECO:0000313|Proteomes:UP000018184};
RN [1] {ECO:0000313|EMBL:CDA45727.1, ECO:0000313|Proteomes:UP000018184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:5226 {ECO:0000313|Proteomes:UP000018184};
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:CDA45727.1}.
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DR EMBL; CBBW010000227; CDA45727.1; -; Genomic_DNA.
DR AlphaFoldDB; R6AX72; -.
DR Proteomes; UP000018184; 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; cd06563; GH20_chitobiase-like; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF13290; CHB_HEX_C_1; 1.
DR Pfam; PF00754; F5_F8_type_C; 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.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000018184};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..775
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004400476"
FT DOMAIN 30..156
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 159..508
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT DOMAIN 638..753
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|Pfam:PF00754"
FT ACT_SITE 333
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 775 AA; 86451 MW; 2112FBA56F6BB479 CRC64;
MKLFAKTAVF IATLLCTTVP KLQAQSANFH VVPLPKVVRS TQAGDFTLNA RTLICYPQGN
KQLKQQATML ANYIKQATGL QLSTTTLAAQ RNCIKLSSVL RHTNPEAYTI RVNSDMVFVD
GASAAGCFYG VQTLRKALPT GVAQQVLIPA TEVNDWPRFS YRGAHLDVAR HFVTADSVRR
FIDMLALHNI NRFHWHLTDD QGWRIEIKKY PLLTKIGARR AQTVIGHNSG QYDGTPYGGY
YTQKDIKDIV RYAAERHITI IPEIDMPGHM QAALAAYPEL GCTGGSYQVW QQWGVTDSVL
CVGNDKTLHF IDDVLNEVVA LFPSEYIHIG GDECPKTMWK RCPKCQARIA AEHLQADGRH
TAEERLQSFL IRHAEQHLNQ LGRQMIGWDE TLEGGLAPNA TVMSWRGEGG GIEAARLKHK
VIMTPNTYLY FDYYQSADKA HEPEAIGGYL PLQHVYSYEP VPRSLAPDEQ QYIIGAQANL
WTEYIKTFKQ VEYMELPRLA ALSEVQWCDA GQKDYAQFVT RLQRLIDTYR LQGYNFAKVI
YNVGVTLATD TTNHCIRATL STIDNAPIHY TLDGTTPTTA SPRYAEPLRI TAPCQLRAAA
FRPWGATHEV QRTFNFSKAT ACPITLLQQP HPKQVYGGAT LLVDGLTASD TNYASGRWIG
FCGNDLEAVI DLGSVTPISR ASINTCVEKG YWLFDARRFE VSASTDGRTF APLAAEDYPA
LTEQSPNQIN THTLQFATTA ARYVKVKVVS EHTIPAWHPG HGNPGFVFVD EIAVF
//
