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Database: UniProt
Entry: U4Q7V6_TEPAE
LinkDB: U4Q7V6_TEPAE
Original site: U4Q7V6_TEPAE 
ID   U4Q7V6_TEPAE            Unreviewed;       414 AA.
AC   U4Q7V6;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   OrderedLocusNames=TEPIRE1_0276 {ECO:0000313|EMBL:CDI40335.1};
OS   Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Tepidanaerobacteraceae; Tepidanaerobacter.
OX   NCBI_TaxID=1209989 {ECO:0000313|EMBL:CDI40335.1, ECO:0000313|Proteomes:UP000010802};
RN   [1] {ECO:0000313|Proteomes:UP000010802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX   PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA   Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT   "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT   Tepidanaerobacter acetatoxydans strain Re1.";
RL   Genome Announc. 1:E00213-E00213(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC         Evidence={ECO:0000256|ARBA:ARBA00001231};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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DR   EMBL; HF563609; CDI40335.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4Q7V6; -.
DR   STRING; 1209989.TepRe1_0254; -.
DR   KEGG; tae:TepiRe1_0276; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_008392_0_3_9; -.
DR   OMA; WQMAAEM; -.
DR   Proteomes; UP000010802; 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   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:CDI40335.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDI40335.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010802}.
FT   DOMAIN          56..377
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
SQ   SEQUENCE   414 AA;  46206 MW;  F7ADA1B1D1023F27 CRC64;
     MADMNYKLLL IIIVLSIVVV YGCESYNNQA VKDQDHIIDQ DADIVDPLKE QIAQMTIDEK
     VGQMVMVGLE GYEKDQYSQE MIEKYKVGGF IFFERNIRDA YQTLTLINSL KEANKENAIP
     LFIAVDEEGG RVTRMPEEFI KLPASRLIGR INNEELCFKI GNVIGEELKS LGFNMNFAPV
     LDIDSNPANP VIGDRSFSSN EQTVSKLGTA TMKGIQTNVI SAVKHFPGHG DTSTDSHIGL
     PVVNCDLERL KSFELVPFAS AVENGADMVM VAHILLPEID EENPATLSKS IITDILRSEM
     KFDKVVITDD MTMGAITENF DIGDAAVKSI MAGADIILVC HDHEKQVKVL EALKQAAVDG
     IITEDELDMH IYRILKLKQK YNLNDEKIES VDVEKINEKI RDILGKDFCA LKFL
//
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