ID Q1ZP57_PHOAS Unreviewed; 887 AA.
AC Q1ZP57;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=VAS14_17656 {ECO:0000313|EMBL:EAS64103.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS64103.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS64103.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS64103.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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}.
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:EAS64103.1}.
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DR EMBL; AAOJ01000004; EAS64103.1; -; Genomic_DNA.
DR RefSeq; WP_005370507.1; NZ_CH902601.1.
DR AlphaFoldDB; Q1ZP57; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_007082_4_1_6; -.
DR OrthoDB; 9763537at2; -.
DR Proteomes; UP000001603; 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: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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..887
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004198921"
FT DOMAIN 35..196
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 541
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 887 AA; 98124 MW; 9C8AC1CB36C9935F CRC64;
MTIKLTALAS FITLAVTGCA TQGNNDQTVV NNLASNLDLN YEVAIQHGAE EGLPCKTLGA
EWASCDLINL TLENKGPAVT NKDWKIYFSS IRQILEVQND QFKVTHVTGD LHTLEPTDKF
DGFAEGEKVV IPYIGEYWTL FENDYMPRAY VTAGNAEPKT IVSTDTANPA DYLTPLKGDQ
FKRVKADNNV LATPETRFEK NSDVNLVASE EVAGTILPTP LSTKLTGDTV SLANGIKIDN
LTLPADMMAA VDARLAQLGV NAQGEYPVKV TILPGSFKKD QQIVGAYKLD VTKKGATITG
FDNQGAFYGM QSLISLMSTG AENSIPTLNV LDAPRFDYRG VMVDVGRNFH SKEAILRTLD
QMAAYKMNKF HFHLSDDEGW RIEIPGLPEL TEIGGKRCHD LSETSCLLPQ LGSGPTSEND
GSGFYSKQDY LDILKYAKAR GIEVIPEIDM PAHARAAVVA MEARYKRLAA EGKMDEANEY
RLMDPQDTSN VTTVQFYDKR SFINPCMDSS AKFVDKVITE IQAMHKDAGM PLNTWHFGGD
EAKNIKLNAG FQDINAAEPT AWTGSIDQSK QDKPYQKSPM CQKLIADGVV SDYDRLPSYF
AERVSAVVNG KGIENFQAWQ DGLKYSKDAK AFDTDNVRVN FWDVLYWGGG ASAYEWANKG
YDVVVSNPDY VYMDMPYEVD PSERGYYWAT RATDTRKMFG FAPENLPQNA ETSLDRDGNG
FASKGTVESK GFHGLSAQLW SETVGNDDQY EYMVFPRVLA AAERAWHKGE WENEYQAGVE
YSQDSNLVNK KALHNEWERF ANVLGQRELA KLDAAGIQYR VPVPGAKIEN GKLAMNVSMP
GLALQYSTDE GKTWNTYNAK AQPSVTGKVE IRAVSADGKR FSRVTSL
//
