ID E4TL09_MARTH Unreviewed; 983 AA.
AC E4TL09;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN OrderedLocusNames=Ftrac_3312 {ECO:0000313|EMBL:ADR23286.1};
OS Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408
OS / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter tractuosus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Marivirgaceae; Marivirga.
OX NCBI_TaxID=643867 {ECO:0000313|EMBL:ADR23286.1, ECO:0000313|Proteomes:UP000008720};
RN [1] {ECO:0000313|EMBL:ADR23286.1, ECO:0000313|Proteomes:UP000008720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 /
RC H-43 {ECO:0000313|Proteomes:UP000008720};
RX PubMed=21677852; DOI=10.4056/sigs.1623941;
RA Pagani I., Chertkov O., Lapidus A., Lucas S., Del Rio T.G., Tice H.,
RA Copeland A., Cheng J.F., Nolan M., Saunders E., Pitluck S., Held B.,
RA Goodwin L., Liolios K., Ovchinikova G., Ivanova N., Mavromatis K., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Han C., Tapia R., Ngatchou-Djao O.D., Rohde M., Goker M., Spring S.,
RA Sikorski J., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Marivirga tractuosa type strain (H-43).";
RL Stand. Genomic Sci. 4:154-162(2011).
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}.
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DR EMBL; CP002349; ADR23286.1; -; Genomic_DNA.
DR RefSeq; WP_013455428.1; NC_014759.1.
DR AlphaFoldDB; E4TL09; -.
DR STRING; 643867.Ftrac_3312; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR KEGG; mtt:Ftrac_3312; -.
DR eggNOG; COG1472; Bacteria.
DR eggNOG; COG1680; Bacteria.
DR HOGENOM; CLU_012120_0_0_10; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000008720; Chromosome.
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; 3.20.20.300; 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; 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 PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADR23286.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008720}.
FT DOMAIN 41..355
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 589..952
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 983 AA; 111471 MW; 9640CC47A681E6C7 CRC64;
MFKKVFSLSI LLVYSVLNSL FSQEIMYPKW VEETYAEMNQ EEKIGQLFMV AAYSNKDEQH
IKNLSLLIEN YHIGGLIFFQ GGPGREINMT NQLQAKSEIP LWIGMDAEWG LGMRLDSTMN
FPKQMTLGAI QNNDYIYKMG AEIARQAKLI GVHVNFAPVV DVNNNIKNPV IGNRSFGEDK
VNVAEKGVAY MKGMQDNGLL ANAKHFPGHG DTDSDSHMTL PIINHSKGRL DELELYPFKK
LIENNVNSMM VAHLHIPAYD STPNKATTLS KNVVTDLLKE ELGFNGLIFT DALNMKGVSD
FYAPGETDLL AFKAGNDVLL FPMDVPNAIN MIKDAIKKGE LPEERLEESV KKILHAKYKL
GLHEGFKKLE PEKIHEKLNS TEAKNLNEKL YAEAATLVRN EKNFLPIHIL DTTNFASLSL
KGDNNNTFQE YLSKYADFTH YHLPKDNMDL GDYSQLINQL SQYETVVVGL HGMNNSASKR
FGLKSEDLLF LQNLSEKANV VLTVFGNAYS LKYLQSFQHI LMMYEDNDIT QKLAPQMIFG
AKPTKGKLPI SVAPEMKAGT GINTKTLNRF GYSNPLDVGM DPKILAEIDA IAQEAIETEA
TPGGQILVAK DGQIVYEKNF GYQTYHKYSK VKDETIYDLA SITKVAATLQ SIMFLYDRGI
IDLDKKISHY LPELKKSNKQ NMTLRNILTH QAGLVPYVPF WRQTHDMFGL KTPMYQNHEA
SLYPNQLASG LYGHQVLGDS IWQWVIDSEL LEKPRWQKNY DYRYSDMGYY IMQKISERMT
NMSYEDFLHE NFYKPMGMST MGFLPLCRFP ETQIAPTEND LVFRNDLIKG WVHDQGAAMV
GGVAGHAGLF SNAKDLAILM QMNLWDGTYG GVRYFSKGTV PYFTKKQFDE NRRGLGWDKP
VEEEGPSPTS HYASPLTFGH TGFTGTAAWA DPEFGLVYIF LSNRVYPDAD NRKLISSNIR
TRIMDVIYQS IFEYESEQEE YVN
//
