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Database: UniProt
Entry: G1VH12_9BACT
LinkDB: G1VH12_9BACT
Original site: G1VH12_9BACT 
ID   G1VH12_9BACT            Unreviewed;       698 AA.
AC   G1VH12;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=HMPREF0666_02695 {ECO:0000313|EMBL:EGW49475.1};
OS   Prevotella sp. C561.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=563031 {ECO:0000313|EMBL:EGW49475.1, ECO:0000313|Proteomes:UP000003086};
RN   [1] {ECO:0000313|EMBL:EGW49475.1, ECO:0000313|Proteomes:UP000003086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C561 {ECO:0000313|EMBL:EGW49475.1,
RC   ECO:0000313|Proteomes:UP000003086};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA   Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. C561.";
RL   Submitted (MAY-2011) 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:EGW49475.1}.
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DR   EMBL; ADCT01000102; EGW49475.1; -; Genomic_DNA.
DR   RefSeq; WP_009012767.1; NZ_JH114152.1.
DR   AlphaFoldDB; G1VH12; -.
DR   STRING; 563031.HMPREF0666_02695; -.
DR   PATRIC; fig|563031.3.peg.2580; -.
DR   eggNOG; COG3525; Bacteria.
DR   HOGENOM; CLU_007082_5_0_10; -.
DR   Proteomes; UP000003086; 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; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..698
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003424385"
FT   DOMAIN          26..150
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          154..505
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   DOMAIN          584..685
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|Pfam:PF00754"
FT   ACT_SITE        335
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   698 AA;  79915 MW;  441C5220911ABE6A CRC64;
     MIKKVFIGAA FLLLSASITQ PVSAQSIIPQ PESITRQQGT FTLAKGLQGV TNLKGEAFKI
     LNQYTSDIMS IPFSSVKKPS ADAPLRLICT GTEQEAAMAA DSVSLQGYEL NVTPTAVTIQ
     ARTPMGLFYG LQTLRQLEKD RQIPCVKITD TPRFAYRGLM IDCSRHFWWK DEIKKQLDAM
     AYFKLDRFHW HLTDGGGWRM EVKKYPRLTE ETAYRTESDW TKWWNGKNRQ YSPDPVRLVC
     WKGMNIHGGY YTQEDIKEIV DYAAARHITI IPEIEMPGHS DEVVYAYPEL SCTGKPYTQS
     DLCVGKEQTY TFMENVLKEV MQLFPSKYIH IGGDEAERRT WKTCPDCQRV MKDYHLKDVA
     ELQSHFTHRI ERFLNDNGRK LLGWDEIMEG TLAPNAAVMS WRGTEAGLTA AKSGHHVVMA
     PQEFCYLNMY QDDPMTEPKA QGGYTRLEKT YNYDPIPAAY KGTSLEKYID GVQGCVWTEF
     IEEPDHLEYM IYPRLLALAE TGWTKQRTGY ADFRQRVITA TDALKRAGYN AFDIRKEKGA
     RPESRSIVQH EALGKPVTYL GRYAEKYRAE GDSTLTNGLR GDWGYLEGRW QGFIDSTGVD
     VVVDMGKVTD IRDVRVDFMH LYESVIYTPE TIELMVSDDG KNFKTIDTVR PGIKASEDYL
     VYPYKWKGDV KGRYVRVKAL SREKDAWIFT DEIIVNQK
//
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