ID A0A1T4TVU1_9BACT Unreviewed; 758 AA.
AC A0A1T4TVU1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=SAMN04488128_106437 {ECO:0000313|EMBL:SKA44553.1};
OS Chitinophaga eiseniae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=634771 {ECO:0000313|EMBL:SKA44553.1, ECO:0000313|Proteomes:UP000190367};
RN [1] {ECO:0000313|EMBL:SKA44553.1, ECO:0000313|Proteomes:UP000190367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22224 {ECO:0000313|EMBL:SKA44553.1,
RC ECO:0000313|Proteomes:UP000190367};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; FUWZ01000006; SKA44553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4TVU1; -.
DR STRING; 634771.SAMN04488128_106437; -.
DR OrthoDB; 726159at2; -.
DR Proteomes; UP000190367; 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; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF13290; CHB_HEX_C_1; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..758
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012323548"
FT DOMAIN 626..758
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT ACT_SITE 350
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 758 AA; 84828 MW; ECD897460EDCEA1A CRC64;
MRRVFVLTLS LALGMGLRTA HAQEKRYPII PYPQQLVPIE GAFTITGATR LVLPANGRLF
ANEVAQLQAL VKQGIGTTLK TATAAAGNAI VLKQDMTLSG EEDYTLQVTP QQLLIGAKSP
TGFFRAIVTL RQLMPSAIEG RTTGNLRSVA IPAMRLKDNP VYSWRGMHLD VSRHFFSVSY
LKKFIDLLAL YKMNKLHLHL TDDQGWRIEI KKYPLLTSVG AWRELNNQDS VCMEKAKENP
DMEIDQEHII QKDGKTLYGG FYTQAQMKDI IAYAAARHVE IIPEIDMPGH MMAAIRAYPF
LTCDGKSGWG KDFSTPICPC NESTFRFAED VYSEIAALFP SKYMHLGADE VEKTSWAASP
VCAEVMKANN LKSVEELQSY FVKRMEKFFH AKGKVLIGWD EILEGGISPT AILMYWRAWV
PDAPVKAARH GNKVIMTPGN PLYFDAQPDR NSLGNVYHFE PVPKGLTARE ARSIMGAQAN
IWTEYIPSEK RADYMFMPRM TALAEVLWTH KQDYDNYLQR LNEQYARLDQ LGVHYRLPDL
DGFTEDNVFV DKGMLEVKAP FTGMTIRYTT DGTIPGLKSP VLPAALPVTA PQTFKLAAFS
PMGNRGDIYT LRYRQEAYAK AVTEKPADSG FRLDYFKGAF KTTAKIKATP DSTFRTDKVI
IPEGLGHGEA FGARLQGYFY APETGIYSFY LTCDDGGMLY IGDKTVVNND GWHAPLQKSG
QIALEKGWHP LKVDFVEGGG GYTLKLEYSV KGQPLQKL
//
