ID F4GYI5_CELFA Unreviewed; 564 AA.
AC F4GYI5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN OrderedLocusNames=Celf_2983 {ECO:0000313|EMBL:AEE47102.1};
OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS NCIMB 8980 / NCTC 7547).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE47102.1, ECO:0000313|Proteomes:UP000008460};
RN [1] {ECO:0000313|EMBL:AEE47102.1, ECO:0000313|Proteomes:UP000008460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellulomonas fimi ATCC 484.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CP002666; AEE47102.1; -; Genomic_DNA.
DR RefSeq; WP_013772128.1; NC_015514.1.
DR AlphaFoldDB; F4GYI5; -.
DR SMR; F4GYI5; -.
DR STRING; 590998.Celf_2983; -.
DR KEGG; cfi:Celf_2983; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_008392_5_3_11; -.
DR Proteomes; UP000008460; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
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; PF00933; Glyco_hydro_3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEE47102.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008460}.
FT DOMAIN 29..347
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
SQ SEQUENCE 564 AA; 59993 MW; 9B1428A4561F71D3 CRC64;
MIDLTAAPFS LDDDGIAWVR TTLAEMGEDE KLGQLFCLIT YTSDPEYLGY LTRGLHVGGV
MLRTMTAADA AATVTTLQST ATVPLLISAN LEGGASQTVQ EATHVGSNMA LAATGSTDHV
RRAATVIGRE ARALGINWAF TPVVDIDLNF RNPITNTRTF GADAATVAAM GAEYVEAIQA
QGLAASAKHF PGDGVDERDQ HLLASVNTMS VEEWDDSFGV VYRAAIAAGV KTVMVGHIML
PAYSRALRPG VADRDILPGV VAEELLNDLL RDRLGFNGLV VSDSTTMAGL ASVLPRSQAV
PRVIAAGCDM FLFTKNLDED FGYMRAGIRD GVITPERLDE AVTRILALKA SLGLHRGTNL
PAQGAAGVLA DPDHSATARE VAASSITLVK EEPGVLPITR ERYPRVLVYD LQNGGSPIGQ
GARAGAVEQF VDALVEAGHD VTRFEPGGGW EGMAAPTTDV TERHDLVLYL ANLSTRSNQT
VVRIEWAEPM GANVPAYVHS VPTVFVSFEN PYHLFDVPRV RTLINTYGSS PVVLETLLAA
LQGKAPFAGS SPVDAFCGQW DTHL
//