ID A4Y4C0_SHEPC Unreviewed; 900 AA.
AC A4Y4C0;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
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};
DE Flags: Precursor;
GN OrderedLocusNames=Sputcn32_1075 {ECO:0000313|EMBL:ABP74803.1};
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP74803.1};
RN [1] {ECO:0000313|EMBL:ABP74803.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 {ECO:0000313|EMBL:ABP74803.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000681; ABP74803.1; -; Genomic_DNA.
DR AlphaFoldDB; A4Y4C0; -.
DR STRING; 319224.Sputcn32_1075; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR KEGG; spc:Sputcn32_1075; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_007082_4_1_6; -.
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 Glycosidase {ECO:0000313|EMBL:ABP74803.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABP74803.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..900
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002676209"
FT DOMAIN 60..225
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 568
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 900 AA; 99521 MW; 664D39D2D14B5C75 CRC64;
MNKTFAATAI LVALGLTACS DVPDAQVVNQ APKPAHASPA SEVNAVSGAL TQTQLQQLGD
TLTATYRVVT NIPDEQCNKA LAEGRCFVAE IDFVPGIDIA SHDWSIYFSQ MRPVQSVQSD
EFTISHVKGD LYRIAPTAAF TGFSKGVKKT LRFRGELWQL SETDAMPNYY LVAEHLAPVL
IASTQVVQDP ETKLEVRPYV EGYTDMVKQY RRTETDKLQP ADAARLFINN QAVSEDAALA
TNAIIPTPQK VQVHGTDKAV SLAAGIKVDY QQLDPTLLTP SQVAAALARL ARLGVAENDQ
GLAVKLQHSA GNEGSYQLDI KANEINIAAA DAAGFSYALS SLASLVDVQD LRVNAMTIED
SPRYPFRGMH IDVARNFHSK QLLLDLLDQM AAYKLNKLHL HMADDEGWRL EIDGLPELTD
IGSQRCHDLA ENTCLLPQLG SGPFAESSVN GFYTKQDYID IVKYAEARQV QVIPSMDMPG
HSRAAIKSME ARYRKLLAED KAAEAKTYLL SDADDKTVYS SVQYYDDNTL NVCMESTYQF
VDKVIDEIAK LHQAAGQPLT RYHIGADETA GAWKQSPQCL AFVANNDKGV KSIDELGAYF
IERISNQLAN KGIEAAGWSD GMSHVRPENM PAKVQSNIWD VIAHKGHSRA NQQANLGWET
VLSNPEVLYF DFPYEADPKE HGYYWASRAT NSHKVFSFMP DNLAANAEQW TDIQHQPFEA
DDRIKLDEAG KKVSGPREEG KAFSGLQGQI WSETIRSDDT AEYMIFPRLL MLAERAWHQA
AWEVPYQYQG AVYNQNSGAF TLAMREAQAK DWQQLANTLG HKEFIKLDKA GINYRVPTVG
AEIRDGKLFA NIAYPGLKLE YRSLNGQWQA YQVGLAVTAP IEIRAIAADG IRKGRSLIVN
//
