ID B1C336_9FIRM Unreviewed; 1524 AA.
AC B1C336;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=CLOSPI_01649 {ECO:0000313|EMBL:EDS74594.1};
OS Thomasclavelia spiroformis DSM 1552.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS74594.1, ECO:0000313|Proteomes:UP000004910};
RN [1] {ECO:0000313|EMBL:EDS74594.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS74594.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium spiroforme (DSM 1552).";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS74594.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS74594.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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:EDS74594.1}.
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DR EMBL; ABIK02000013; EDS74594.1; -; Genomic_DNA.
DR RefSeq; WP_004610146.1; NZ_DS562852.1.
DR STRING; 428126.CLOSPI_01649; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR GeneID; 67387756; -.
DR eggNOG; COG1538; Bacteria.
DR eggNOG; COG3250; Bacteria.
DR eggNOG; COG3507; Bacteria.
DR eggNOG; COG3525; Bacteria.
DR eggNOG; COG3568; Bacteria.
DR HOGENOM; CLU_247575_0_0_9; -.
DR Proteomes; UP000004910; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd06568; GH20_SpHex_like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 3.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 2.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
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 PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF07554; FIVAR; 5.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDS74594.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000004910};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1524
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038791107"
FT TRANSMEM 1501..1519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..185
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 189..513
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT DOMAIN 825..1040
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT REGION 1470..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 369
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 1524 AA; 169546 MW; 1D80BD4071D5BB25 CRC64;
MSLIKKFKMK KMLALTLAAF MSFTTVTAMP IQPVNAVEEP ASLERQLIPL PVDYEVTQDK
FTISEDTNIY VKGLDDKQTD ELYENVGEYL ASKLRPSTGY ELPVIKGDNE GTGNIAIVIS
DSESDLGEEG YKIKTTEAGV EITANQPAGA FMAVQTVRQL LPADIEKTEL VEGVSWVIPC
SSINDKPEYE YRGSHLDVTR HFFSVEDVKR YIDNMAQYKM NKLHLHLSDD QGWRLEIKGE
MYGESLSKLN TIGAQTSTSI NGIKAGQYTQ EDYKEIVAYA ADRYVEIIPE FDMPGHSWAA
LVSLNFLNSS EDGKPHSGNY DNTKPYEGID VGFSTFECRN EKTYEFIDEV FRQVAAISPS
KYIHIGGDEA HSTSSEDYAY FMNRVTEIAK KYGKTPIGWQ NYDGVAEDKE GTVTQFWSTG
NAKLKDGIKY VVSPADYAYM DMKYDASCEL GLQWAGYNSI EDTYSWDPTN YGDKENIVGI
EACLWSETLA NNDHLDYMAY PKILSHAEIG WTPKELRSWD TYKPRLIAHG ERLENQGIKF
NKDEDIWEVP YEPVNGMWNL DEGKGNTITD TEGKYIGTFQ GEVGWTDGVN GKALDFNRKG
YVDLELGKVK GDWTVACWVK NGTNPHTNAV LFGGSEGDIK LEQYKNTKKL GVSIYGVVDS
SFDYSLSEGE WKHVAFVGDS TGTSLYVDGQ YIDKVSTTIN CPVQRIGAAV NNDINSPGNM
SGSMDELNIY NRALEAEEIK AIYDGSVVII EKETLKAEID AAESLEKDEY TEKSWKELED
ALAVAKEVYA NDEATQSQIN SAYYALVKAR EGLKKELKSN EINIASFNIA ANRHPNIAAI
SDLMEEKQIT VAGVQEVDVF TSRNNYDMMQ EFVNQGYFGY SHFQKAIDYG GGEYGVGIVS
QNELSGQSGA SLPSLPGIEG RAYARAEFEK DGKTIAIYST HLSYEDSDIR RQQIETIINA
MDADPTPYKI LTGDFNTGDS NSEFYPFLRN YNIANGKDDV WLETIGDTAE GARREIDNII
TTRNIKINTV ETVNEGLSDH YMLYAQCELL DEEVPNRQLL GYTLEKAESL PSDSYTEASY
AVLAKAIEEA KGLAADATQD QINAMIDKLE VVMDQLVESN KIINDSEVGT GVDQFNFVGE
WGVSQGYLDR FYNGDEHWFN WARYQEGDIV PYFTITFEGT GIELYGNKDT MMGIYDITVD
DGEVIQVDAY NPSTLYQQLL FSVTGLEYGQ HTIKVSATRN KNENSTSSDI EIDYAKILYD
QDIQEVDKTA LKIAVDLANA ITDKDLEKVI PVVANEFIAA RDEANAIYND ASATQDEVNA
AFDILASAMH MLDFVKGDKT ALKAFIDDVT GLDSSKYSTD TWAAFEKELN EANVVYNDDN
AMQEEVNNAY KELVTAFLNL RLIPDKSLLE DLINQAEGLN SVNYTKATFN GLTKALDEAK
VVFDDPNVTQ EQVNNAKDLL EKAIAGLQAN PSTPSNVDNT VSTPLDNGDT TASVKTGDGS
LVGMFATIAL LSVAGYTVLR RKEN
//
