ID F3ZRT1_9BACE Unreviewed; 547 AA.
AC F3ZRT1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=Bcop_1832 {ECO:0000313|EMBL:EGJ72020.1};
OS Bacteroides coprosuis DSM 18011.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ72020.1, ECO:0000313|Proteomes:UP000018439};
RN [1] {ECO:0000313|EMBL:EGJ72020.1, ECO:0000313|Proteomes:UP000018439}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ72020.1,
RC ECO:0000313|Proteomes:UP000018439};
RX PubMed=21677860; DOI=10.4056/sigs.1784330;
RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type
RT strain (PC139).";
RL Stand. Genomic Sci. 4:233-243(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001167; EGJ72020.1; -; Genomic_DNA.
DR RefSeq; WP_006745176.1; NZ_CM001167.1.
DR AlphaFoldDB; F3ZRT1; -.
DR STRING; 679937.Bcop_1832; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_007082_5_1_10; -.
DR OrthoDB; 1090159at2; -.
DR Proteomes; UP000018439; 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: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 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 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 PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 2.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:EGJ72020.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGJ72020.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018439};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..547
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003303810"
FT DOMAIN 44..166
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 170..513
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 355
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 547 AA; 63106 MW; E1877D8D2A183DC2 CRC64;
MKTQYSLIKR TSLITLLITA LFTTYSCAND DDNNSQPNIS SKNIEIIPQP VSLEYGSQRI
EMPSVVSISK DIPSTMQKLL EKSITDYKVA SSINIEKNES AFISTKIDNS LSEEEYELDI
TQKSILITHS TQQGLLWGIQ TLRQVLMQAE SSTKGDFSIP TLSIKDTPKY AWRGFHIDLA
RHMFSLDYLK KVTDCLSLYK INKIQLHLTD DQGWRIEIKK HPNLTTVGGW RHFDEYDEEC
IKLSHTDASY TIDERYIRNG KEYGGFYTQD EIKDFVTFAT SVGIEVIPEI DMPGHFSAAI
KAYPELSCTG SSGWGEEFSY PVCAGKAKNH PFLYDILDEV MTLFPSKHFH IGADEVEKNN
WKKCEDCQRL IAEENLMNVE GLENFFVNNI NSYLNKREKS TMAWDDAFYK KEPQEMIYTY
WRDWLPNQAG TITQAGFPVV FMEWGNFYLS ATPSDEQLQS LYNFKFEPKF KGIVKSNILG
FQACIWTEMI PNEQKLGHHL FPSIQAYTEV AWGTASNWDS FKKKMNWHLK HLTKEGFYVR
TPDFIKK
//