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Database: UniProt
Entry: F9Z450_ODOSD
LinkDB: F9Z450_ODOSD
Original site: F9Z450_ODOSD 
ID   F9Z450_ODOSD            Unreviewed;       672 AA.
AC   F9Z450;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Glycoside hydrolase, family 20, catalytic core {ECO:0000313|EMBL:ADY31354.1};
GN   OrderedLocusNames=Odosp_0251 {ECO:0000313|EMBL:ADY31354.1};
OS   Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / CIP 104287 / JCM
OS   15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC   Odoribacter.
OX   NCBI_TaxID=709991 {ECO:0000313|EMBL:ADY31354.1, ECO:0000313|Proteomes:UP000006657};
RN   [1] {ECO:0000313|EMBL:ADY31354.1, ECO:0000313|Proteomes:UP000006657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6
RC   {ECO:0000313|Proteomes:UP000006657};
RX   PubMed=21677857; DOI=10.4056/sigs.1714269;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A., Hammon N.,
RA   Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA   Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA   Rohde M., Detter J.C., Woyke T., Bristow J., Markowitz V., Hugenholtz P.,
RA   Eisen J.A., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Odoribacter splanchnicus type strain
RT   (1651/6).";
RL   Stand. Genomic Sci. 4:200-209(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
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DR   EMBL; CP002544; ADY31354.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9Z450; -.
DR   STRING; 709991.Odosp_0251; -.
DR   PaxDb; 709991-Odosp_0251; -.
DR   KEGG; osp:Odosp_0251; -.
DR   eggNOG; COG3525; Bacteria.
DR   HOGENOM; CLU_010969_2_0_10; -.
DR   OMA; YWTGKEI; -.
DR   BioCyc; OSPL709991:G1GRN-248-MONOMER; -.
DR   Proteomes; UP000006657; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06564; GH20_DspB_LnbB-like; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
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; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR   PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADY31354.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006657}.
FT   DOMAIN          37..159
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          162..480
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        323
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   672 AA;  76861 MW;  2332AAEC64BE4B5E CRC64;
     MNMMKQKTNF AGLVKRVTCL ICGICFCFGI YAQQQKPFVI PELKEWKGAT GFFMPKQSVR
     IIYGAPGLQK IARQFAADYK ALFGVLPEIA EGKPCKGDFF FTIKRDKKLE KEGYDIVIGD
     YVKVSANEPV GVYWATRTLL QMGEQYKNGN LPKGHIRDWP DYGIRGLLID CGRKFIPMNY
     LRDLACIMSY YKMNFMHVVL NNNGFKAYFN DDWNQTYAAF RLECETYPGL TARDGYYTKK
     EFVHFQEEAA ERFVEIIPEI DIPAHSLAFS HYKPELGSKE YGMDHLNLSH PEVYSFVDAL
     FKEYLDGENP VFRGPRVHIG TDEYSNKKKE VVEQFRAFTD HYIKFVEGFG KQACVWGALT
     HAAGETPVKS DNVIMYAWYN GFANPKDMVQ QGYNLISIPD GLTYIVPLAG YYWDYLNTER
     LYKQWTPAHV ADVVFEEKDP AIIGGMFAVW NDIVGNGISV KDIHHRIFPA LQTIAVKTWN
     IAPAFSYTEF ETKRQKLSEA PDVNQLGRIG DDENSLVYET SSITPGSELP YTEIGYDYTI
     TFDMEAANEN YGTELFRSPN AVFYLADPVK GMFGFSRDGY MNTFAFRPYP GEKISVKITG
     DALSTSLFIN GQLIERMGIE KRYLNEAEKQ NNFIRTLVFP LKNAGNFKSK ITNLKVYNRL
     CSHGTRAKTD RH
//
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