ID   A4C3P8_9GAMM            Unreviewed;       759 AA.
AC   A4C3P8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE   AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00030512};
DE   AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|ARBA:ARBA00033000};
GN   ORFNames=PTD2_01386 {ECO:0000313|EMBL:EAR30180.1};
OS   Pseudoalteromonas tunicata D2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR30180.1, ECO:0000313|Proteomes:UP000006201};
RN   [1] {ECO:0000313|EMBL:EAR30180.1, ECO:0000313|Proteomes:UP000006201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D2 {ECO:0000313|EMBL:EAR30180.1,
RC   ECO:0000313|Proteomes:UP000006201};
RA   Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA   Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA   Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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:EAR30180.1}.
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DR   EMBL; AAOH01000001; EAR30180.1; -; Genomic_DNA.
DR   RefSeq; WP_009836481.1; NZ_AAOH01000001.1.
DR   AlphaFoldDB; A4C3P8; -.
DR   STRING; 87626.PTD2_01386; -.
DR   eggNOG; COG3525; Bacteria.
DR   HOGENOM; CLU_007082_5_0_6; -.
DR   Proteomes; UP000006201; 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; 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   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..759
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002667062"
FT   DOMAIN          25..157
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          160..505
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        336
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   759 AA;  85384 MW;  7AFCB36A20901D37 CRC64;
     MYYKILTSIS VLVFSAWLWA APSTISIVPE PKQTIVSKGV FSLNNQTKIS YDSDKSKPTA
     TMFWQTIAPV TGYQQPITQR SVVGKNHIHF QLDSTLTTPE SYQLSVSVEQ VRIRAADVAG
     LFYGMQSLLQ LLPPDIYANH PINQLSWDIP AVEINDQPRF SYRGMHLDVS RHFFNVDFIK
     SYIDWLAFHK LNVFQWHLTD DQGWRIEIKT YPKLTEVGSI RNQTVLGHTY DYQPLFDTTA
     VKGFYTQAQI KDVVAYAAAR HVMVIPEIDI PGHSTAILAA YPELGCSGKR PVVEDNFGIF
     EAVLCPTEQT FAFLQQVYQE VATLFPAPYI HVGGDEVIKK QWLASPFVQQ LMQELQLTST
     EQVQSYFIGR VSNIVTALGK KMIGWDEILE GGLAPNALVT SWRGEDGGVA AATLGHQVIM
     SPYQFVYFDA YQSLSQREPK AIHGLTTLKD VYLYEPIPAQ LPASQHHLVL GAQGALWTEY
     IKTPQQAQYM LFPRIAAFAE GVWSQPAQRN WSLFTQKLPL LFARYQAQNI HYALSHLVPD
     IAIKQVNSGQ SQLTIANQLD GQIQVKLTNE TLDHIYSEPL LVDSNKQVVS VSARLFAPKL
     GLYSLPVQVS FAHHKAVGKP ITLKYPAQSD GLQKLNDGIF AFDQFYRADN FAIFYDSDLE
     AVIDLENKTS FHQIVMGIDA GRHRQLHPPI AISVWVSNDK QNWQRVTQLN ASEINGPLLS
     FAVGKQIARY VKVHAVNAKN STDPQIPKLP LYIDEIAIF
//