ID A0A161S7F1_9FLAO Unreviewed; 960 AA.
AC A0A161S7F1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=AV926_09145 {ECO:0000313|EMBL:KZE81064.1};
OS Myroides marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Myroides.
OX NCBI_TaxID=703342 {ECO:0000313|EMBL:KZE81064.1, ECO:0000313|Proteomes:UP000076630};
RN [1] {ECO:0000313|EMBL:KZE81064.1, ECO:0000313|Proteomes:UP000076630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L41 {ECO:0000313|EMBL:KZE81064.1,
RC ECO:0000313|Proteomes:UP000076630};
RA Hong K.W.;
RT "Whole genome sequencing of Myroides marinus L41.";
RL Submitted (JAN-2016) 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 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:KZE81064.1}.
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DR EMBL; LQNU01000054; KZE81064.1; -; Genomic_DNA.
DR RefSeq; WP_038987899.1; NZ_LQNU01000054.1.
DR AlphaFoldDB; A0A161S7F1; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000076630; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..960
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007826283"
FT DOMAIN 39..352
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 469..545
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
FT DOMAIN 579..936
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 960 AA; 107617 MW; 5D8BEABD46555664 CRC64;
MKRLTVVLLL IASSAFGQSK VNVTRQTQWV DSVYNKLSVE ERIGQLFMVA AYSNKNEAHV
QSLEKLVQEQ HIGGLIFFQG GPVRQANMTN RLQALSSVPM LVGIDGEWGL NMRLDDTYRF
PFNMTLGAVQ DLDLIERVGV AMALQTKRLG MQFNFGPVLD ININPKNPII GVRSFGETRE
IVTERASAFT KGYQSQNIFA TGKHFPGHGD TSTDSHHKLP VIDFDKGRLN RVELYPYKKL
FEEGLSSVMI AHLNLPAYEP NDIPTSLSYN IVTKLLKEEL GFEGLIFTDA LNMKAAANYL
KPGEVDLAAF KAGNDLLLFS EDVPTALTKI LESYNAGDIT EERLSHSVKK VLAYKYKSGL
TKFTPIEVNK LVEDLNAPVY DDLNQKLYQE AMTVAKNEDR LLPFKNLEKQ KIAYMRLGDD
SGADFLNMLR NYAEVTELTD VKPDSLGDLS QYSSVIIGYH KVDNPWRKHD MSDAEKAMVR
NLSAKTNTVL VSFAKPYALE TVPLDKVNAL VVGYQNNKFA QEAAAQVIFG AIEGKGKLPV
SINKNFTVGT GIHTKAINRL GFSTAANEGM DPNVLSKIDA IAQRAIDKRY TPGIQVLVAR
HGKVVYQKSF GYHTYDKKTT VQNTDIYDLA SLTKILGTLP VLVKMYDEHK VRMDSKLGQL
VPAMKHTDKE DITFRDLLTH QSGLTAWIPF YKRTLADNNR PDPSLYSYFY TPEYPTQVSE
NLYIKKGYTD EMLKQIGEST LSTKKDYKYS DLGFIMMKEF IESKYHKPLD QVADSEYFSK
IGAWRMTYNP LRKFDINVIP PTEEDNYYRY TTVQGYVHDM GAAMQGGVSG HAGLFGSALD
VAKMMQLYLN KGEYGGDRFF SVNTFDAFNE CVYCTKGSRR GVGFDKPQKP GSAGPTCGCA
SMSSFGHTGF TGTMAWADPE KDLVYVFLSN RTYPDSNVNN LSKGNTREDI QQVIYESIKN
//
