ID A0A1U9NFP1_9GAMM Unreviewed; 847 AA.
AC A0A1U9NFP1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B0D95_05310 {ECO:0000313|EMBL:AQT62277.1};
OS Cellvibrio sp. PSBB023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT62277.1, ECO:0000313|Proteomes:UP000189646};
RN [1] {ECO:0000313|EMBL:AQT62277.1, ECO:0000313|Proteomes:UP000189646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB023 {ECO:0000313|EMBL:AQT62277.1,
RC ECO:0000313|Proteomes:UP000189646};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; CP019799; AQT62277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9NFP1; -.
DR STRING; 1945512.B0D95_05310; -.
DR KEGG; ceb:B0D95_05310; -.
DR Proteomes; UP000189646; 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:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02847; E_set_Chitobiase_C; 1.
DR CDD; cd06569; GH20_Sm-chitobiase-like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR004866; CHB/HEX_N_dom.
DR InterPro; IPR004867; CHB_C_dom.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF03173; CHB_HEX; 1.
DR Pfam; PF03174; CHB_HEX_C; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM01081; CHB_HEX; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000189646};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..847
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012707957"
FT DOMAIN 27..181
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 530
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 847 AA; 94250 MW; 576DF26CA47C15EC CRC64;
MLCLCLALST GQALANLSAN DLKKFGDKAE LRFATVSNFG QEGTFDALVT VNNHSAIALP
KGKANWKIYI HSVKRILSTS STELTFKRLQ GDLYEIAPTD AFQGLMPGKT LGFPYKARGH
IVSYSDFMPR AFIANTAGEY AVFANTDTED LTQFIDPFTR PEQLLRFDTP KDLYSVVTTT
SRYESNLAVN LSDATAETAK IVPTPKTVTY SKGSANINHE WSIIEVGGLA FEADYLQQRL
RDSGLLLNKG IKNSSHKNRF IELTIDKKIA KTEAYELNIT SEKVVISATS PAGVFYGVQS
FLSLLPAEKS ATQQIPALRV FDEPRAGWRG MHYDLARNFH GKDAVMELIE QMGRYKLNKL
HLHLTEDEGW RIEIPGLPEL TGVGAFRCFD LTETRCLMPQ LGSGPDKASA GNGYLTAADF
TEIIKYAAQR HIDVIPEIDM PGHSRAAIKS MEARYKKLIA EGKKEDAGRY LLSDPKDQSQ
YLTVQSYSDN SVNVCLPSTY AFIEKVTYEL QQMYRKAGQK LTVFHMGGDE VGVGSWTQSP
ACNELFANSE NGVSGVADLK PYFVQRIAEI TNKRGLDLMG WEDGLMYDPN NTFNREQLVN
KRVIANAWDN IWEAGVADRA HRLANNGYDV VISGATHLYF DHPHEPHANE RGYHWATRYI
DIAKVFGFMP DNLYANADRT FIGGEISNLN ALVGRILPPL EKPEHVLGMQ GQVWTETIRT
KSQLQTMIFP RVIALAERAW FKAPWEGNPV NTQARDAEWK TFAATLVTKE LPKLEQSGLA
FYLPPPGAIR IDNTLKANTS LPGLTIEFSL DGGKSWSPYQ QNTSIDDGAI HLRSRLNSVV
SATAILH
//
