ID U4K583_9VIBR Unreviewed; 874 AA.
AC U4K583;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 Name=hex {ECO:0000313|EMBL:CCO60477.1};
GN ORFNames=VIBNI_B0677 {ECO:0000313|EMBL:CCO60477.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO60477.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO60477.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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; FO203527; CCO60477.1; -; Genomic_DNA.
DR AlphaFoldDB; U4K583; -.
DR STRING; 28173.VIBNI_B0677; -.
DR KEGG; vni:VIBNI_B0677; -.
DR PATRIC; fig|1260221.3.peg.4324; -.
DR eggNOG; COG3525; Bacteria.
DR OrthoDB; 9763537at2; -.
DR Proteomes; UP000016895; Chromosome 2.
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 Glycosidase {ECO:0000313|EMBL:CCO60477.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCO60477.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..874
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004650397"
FT DOMAIN 32..200
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 546
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 874 AA; 95860 MW; C3EA5F4BD2067A5A CRC64;
MKFKVTALTM ALALASSGVH AQTQQDLKAT ADSLNVSTSL VVNQPTDSKA ECPWGLCYRA
EITITNTSDK AVNKDWDLYF PSIHRVLDTR GDLFTITHID GDLHRVSPTA KFNGLQPGES
VTVEYDAEYW QIVNSDFMPN YYISADGLKG ELIKNTAVKE ADTGFEDLSG FLTPISNDPA
DTDQWRRTAD DKTNVATAGS RFEKNSDVAD LGQAAVSAQI VPTPVELTIQ TGTIDIAAGL
NIKPVNNALR ADQVEAVNAR LAQLGVATNA GVEVKAISNA GHQAFVGREV KGAYTLKVDA
TGVTVVGRDN EGVFNGLQSL ASLVTVGSSE LPKVTVDYDA PRFDYRGMHM DVSRNFQTKE
QVLKFLDQMA AYKMNKFHFH LADDEGWRLE IPGLPELTDV GAKRCHDLDE TTCLLPQLGS
GPDAAAEKQY YSVADYVEIL AYANARNIQV IPSMDMPGHS KAAVVAMEAR YKTYAAQGDL
AKAEEFLLTD PNDTTKYFSV QNYTNNTINP CMESSFKFMD KVIGEIVAQH NNAGQPLTDY
HIGADETAGA WVDSPICQQM FAVEWNGINN VEDLGPYFIQ RISWILEKYS LTLAAWNDGL
KHGEYINPYT LAGDKTSAYA WSTLFWGGAN ETHTIANTGY EVVVSAPDTT YFDFPYEVDP
AEPGYYWGSR ETDTREVFGF MPENLPANSE TLTDRMGAPM TYAAADGVAL NKKFKGIQGH
LWSETIRTAR QQDFMAFPRL LAMAERAWSK ASWELDYDST ITFKTNVDGY VGTSHVDTAT
RDAEWEVFAN TLGYKEFAKL DQAGVYYRLP VPGAKIEGGK LVANSAFPGV TIQYSTDGTT
WQNYDAANQP AASVGVKVRT VAANGRVGRS IDVK
//
