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Database: UniProt
Entry: A0A0Q5UA15_9FLAO
LinkDB: A0A0Q5UA15_9FLAO
Original site: A0A0Q5UA15_9FLAO 
ID   A0A0Q5UA15_9FLAO        Unreviewed;       969 AA.
AC   A0A0Q5UA15;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=ASG38_14390 {ECO:0000313|EMBL:KQS45803.1};
OS   Flavobacterium sp. Leaf359.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1736351 {ECO:0000313|EMBL:KQS45803.1, ECO:0000313|Proteomes:UP000051024};
RN   [1] {ECO:0000313|Proteomes:UP000051024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KQS45803.1}.
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DR   EMBL; LMPW01000015; KQS45803.1; -; Genomic_DNA.
DR   RefSeq; WP_056073390.1; NZ_LMPW01000015.1.
DR   AlphaFoldDB; A0A0Q5UA15; -.
DR   STRING; 1736351.ASG38_14390; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000051024; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
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; PF00144; Beta-lactamase; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051024}.
FT   DOMAIN          43..359
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          592..945
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   969 AA;  109899 MW;  0AB3EEB4FED78D22 CRC64;
     MRYFVIALLF ISQIAFSQLR EPKLVLDRTK ETIWVDSIYN KMTLQERIGQ LFMVAAYSNK
     DSVHFNAIDK LIREQHIGGV IFFQGGPVRQ ARLTNRFQSK SKVPLFIGID AEWGLAMRLD
     SVIRYPWNMT LGAIQDMKLI EKVGEKYGQQ SRRMGVQFNF APVLDINTNP KNPIIGNRSF
     GEDKMNVTER ALALMKGIQN QGVFATGKHF PGHGDTETDS HHTLPMLNFT KQRINDIEFY
     PYKKLFREGL ASVMVAHLNV PSLEPKENYP TSLSYNVVTN VLQNELHFKG LIFTDALNMK
     GATNFKQPGD IDLEAFKAGN DILLFAENVP LALEKICVAI QDTVISEKRL EQSVKKILRY
     KYLAGLNNYK PVEIPYIYDD LNNADAQALQ YQLYENAVTV LKNENEILPI KDVANEKIAY
     VKLGDDTNTS FLNTLRQYTE VTEVSNDSLH LLIDDLKKYT TVIIGYHKAD GAWKKHDFTV
     DELVKIQEIA KNNKVILDIF TKPYSLIPIN SFSDIEGLVV SYQNSDVAQN VSGQLIFGAI
     DAKGKLPVSI GTTFKVNDGL KTKKLNRLGF TAAENVGMSS KALARIDLIA NNAIERQMTP
     GIQVLVARKG KVVFQKSYGY HDYKNEVKVK NSDIYDVASL TKIVSTLPDV MQLYDQKKIT
     LDTRLGTMLP AFENTDKKNI TFKELLSHYA RLQPWIPFYQ ATLNADKKPS DKYYKNTLTP
     EFSLQVAENL FLRNDYKDTI IKKIAESKLL PKKEYKYSDF TFIILKEYLE KETGKKLDVL
     SEENFYKKLG ANSTTYNPLR KFDMSVIPPT EEDKYFRYQT IQGYVHDMAA AMQDGVGGHA
     GVFSNSIDLA KIMQMYLQKG NYGGIQFFSP ATFDTFNTCY FCKEGNRRAL GFDKPQLPGT
     SGPTCGCTSK SSFGHTGFTG TMAWADPEEE LIYIFLSNRT YPDSNAPNTL SKENVRENIQ
     KVIYDAIEN
//
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