ID S4XU68_SORCE Unreviewed; 901 AA.
AC S4XU68;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 ORFNames=SCE1572_16160 {ECO:0000313|EMBL:AGP35901.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP35901.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP35901.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP35901.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(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; CP003969; AGP35901.1; -; Genomic_DNA.
DR AlphaFoldDB; S4XU68; -.
DR STRING; 1254432.SCE1572_16160; -.
DR KEGG; scu:SCE1572_16160; -.
DR PATRIC; fig|1254432.3.peg.3637; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_007082_4_1_7; -.
DR Proteomes; UP000014803; Chromosome.
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 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 InterPro; IPR022357; MIP_CS.
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.
DR PROSITE; PS00221; MIP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 53..203
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 566
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 901 AA; 95619 MW; 51617AD2F57084DC CRC64;
MAGCGDDGTS SSTASTTMST STGNGGGGGG GGTGGGGGTG GGGGSAQERP SGADFAVTWS
VLDNHKNPAV SFGSELTIEN RGKVALGNSG WTLYFNFVRL IVPESLPPGV KVTHINGDFF
KLEPTEAFQP LEPGQSAVIP FDGSYWAIKE TDAPAGYYFV FTDGEGVASA PEAVGSEAVA
PFVEKKQTDR FPGDMTPVPT AASRYDENLA VRLLPAGDVD RVVPTPVLLE AGDGELSLSS
AVPIYHAAGL EGEAAFLAEA LGALLGAAPE VREGAPPAGT AAIALATGAI DVGGQPKQAG
DEAYRLTVTP EGVEIVGSDA AGVFYGIQSL RALAPVEAYR TAKPEIAIGA VTVEDAPRFG
YRGMHLDVAR NFQRKEAVLK LLDVMAFYKL NKFHFHLTDD EGFRFEVSGL PELTEVGARR
GHTLDDRDQI VPSFGSGPDP ASPSSSGSGH YTRAELVEIL RHAKARHIEV IPEIDMPGHA
RAAVKAMEAR YARLAAEGDV EKAEEFLLSD LEDPSQYMSV QMWTDNVVNP CRESTYRFLR
KVVDDVVAIY AEAGATLTTI HTGGDEVPDG VWEQSPSCEA LLGQAPGGVE SVDDLASHFL
RELNAIVASH GLVTGGWEEI ALKKVQAEGG VDKEANPEFV SSNFRAYVWN NVWGWGDEDN
GYKLANAGYP VVLSNATNLY FDLAYDKDPA EPGYYWAGFV DTRKPYEFVP FDVYKSAHAD
RMGNPIDPAE MFRDHVKLTD AGRANVLGIQ GQLWGENAKG QGAMEYLIFP KLIGLAERAW
APDPAWAAEE DGAARAGLLA EAWSRFANSL GQRELPRLDH LSGGVDYRLP LPGARVEDGK
LVANVAFPGL QIRYTTDGAE PGADSAVYEG PVAVSGVVKL RTFDTRGRGS RTSVLDPDGS
Q
//
