ID R5PD21_9BACT Unreviewed; 729 AA.
AC R5PD21;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=BN465_01402 {ECO:0000313|EMBL:CCZ12109.1};
OS Prevotella sp. CAG:1092.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262919 {ECO:0000313|EMBL:CCZ12109.1, ECO:0000313|Proteomes:UP000017987};
RN [1] {ECO:0000313|EMBL:CCZ12109.1, ECO:0000313|Proteomes:UP000017987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1092 {ECO:0000313|Proteomes:UP000017987};
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:CCZ12109.1}.
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DR EMBL; CAZL010000252; CCZ12109.1; -; Genomic_DNA.
DR AlphaFoldDB; R5PD21; -.
DR STRING; 1262919.BN465_01402; -.
DR Proteomes; UP000017987; 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; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF13306; LRR_5; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCZ12109.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017987};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..729
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004399945"
FT DOMAIN 219..345
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 352..698
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 516
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 729 AA; 82080 MW; 1CBFD98FA3CD491F CRC64;
MKRLFLLSAT ALMATMMSAQ TAARMDSLKP EQKAMAVSLK LTGELSTDVK GDYRQMRDLC
FQVRNIDLSD AQSTIIPKNA FHSRHQLQNI ALPKVLKTIG TQAFFACDKL QSVTIPATVE
TIGAAAFSGC KSMTKLTIEG NPNIGEYAFA RLSELKTVRV KSKVPPKAMA SSFYGIARGS
VHLIVPKGSE KAYMKATGWS SFYAEPKYAK EVSNPMECIA PMPQEVNVQK AKTLNVQTAW
NIVVSHNDGA GTILNNEVEQ AREMLNNRIG NIVNSRQRGI QLVLGIDSSL DDDEAYTMAV
DAKGVTINGK TARGVFWGLM TLDQILRGSG VKECVDAIPH LTIKDTPRTH VRELMVDPAR
TFIPFEELKA FVPEMARYKL NALHLHLVDD QAWRIEIKKY PQLTQQASSR WGQDDLLAPY
KGYYTQEQMR ELVKFAARYH VEIVPEIEMP GHEVAAISVF PELTCHQRQV PIRTTCGVSN
ELLCPGNEFT YEFLGNVFKE LTDIFPSKYV HLGGDEAGNP ALDCWTDCPK CQALKTKLGI
TTTDRSENWK LQGYLFDRII SLLRDTYHKT PMFWYETDFK KIQPGCVTFA WRNGLTEKAL
ETAVENNARI MLCPGEHCYF DYPMANGDMP EVNWGMPVTT LKDAYSLDPA WGHDKNFENN
NLFGVAGTLW SECITSPERI YYQAYPRAIA LAEAGWSQQE NRSWESFLKR MQPLANDMMR
RGISFSMEY
//
