ID L1MJH7_9BACT Unreviewed; 1200 AA.
AC L1MJH7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=HMPREF9999_01028 {ECO:0000313|EMBL:EKX91438.1};
OS Alloprevotella sp. oral taxon 473 str. F0040.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=1035197 {ECO:0000313|EMBL:EKX91438.1, ECO:0000313|Proteomes:UP000010460};
RN [1] {ECO:0000313|EMBL:EKX91438.1, ECO:0000313|Proteomes:UP000010460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0040 {ECO:0000313|EMBL:EKX91438.1,
RC ECO:0000313|Proteomes:UP000010460};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKX91438.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMEK01000054; EKX91438.1; -; Genomic_DNA.
DR AlphaFoldDB; L1MJH7; -.
DR STRING; 1035197.HMPREF9999_01028; -.
DR PATRIC; fig|1035197.3.peg.845; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_273500_0_0_10; -.
DR Proteomes; UP000010460; Unassembled WGS sequence.
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; cd06563; GH20_chitobiase-like; 1.
DR Gene3D; 2.80.10.50; -; 2.
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; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 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:EKX91438.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010460}.
FT DOMAIN 156..288
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 293..666
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 471
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 1200 AA; 134070 MW; F83260B93127021F CRC64;
MPKVSTAQEV HWYLLKFTNS GLVVEASKAN SGARLAAMTG VDAQLWKVEG SAAEGYTFTN
KAGLQLYVTN TQEKGMVEAA KQHANNKFSI LPCKTANFTS SFEIHPKANT QVGFNQWGGA
GAGHPIGLWG SSKDREGNNA LTFETTAALD VYKNLPPLVP YPQNINIQEG KNLDLRNLKV
ITSPVDSLKG MVHEFAEEVK SRLGLTLSLQ SSPSAAADGM VALITDKSVA GAEAYTLSIT
EKHIEIKASH RAGFFYGLQT LRQLMTKAFY PKNGAQRVWT LPVLDIKDKP LLSYRGYMLD
IARHFFDKTE VKRILDIMSF YKMNRLHWHL TDDQGWRIEI PEYPKLTQVG SRRKGSFVSD
GTDPHFFDDT EYGRGMYYTL DDLREIVAYA AERNIEIIPE IDMPGHMVAA LAAYPELSCY
PNRTYKVRVT AGISKDVLNI GDDKVIDFLK TVLDNVAKVF PGRYIHLGGD ECPTDRWKEN
ALCQQRIKDN KLNGVGELQP WLVHELAVYL KKKYNKDIVA WDELIETKTD NYWNRHKGEV
SPLIMAWNLG RDGTGRWTDW TDILAASKGF HTVIVPYNVL YLDWMQVTAD QADVNEGYRG
GWGDGSVNSV EKIYNFDPLA RLRSVGKTEF GLGVQGNMWT ETTNNNAELE YQLLPRLLAI
SEIGWLPNNQ KDWLSFFYRL QQHSVVFEDR KMTYAKHFFL KESKTPLQEK VDEAEKLLAD
TRAGEVGYAP KATCDALANA VTAAKAAAAT EEAQQLEAMT QALAAFKAAP ITQPVAGKVY
RLISASTYYK AKYAGATLYA DGTTAVRVHY TDQQAPEELF TFVEANGGWI MQSVHNKQEV
TISSYNQPLR FVKKNATPIR IDRAAVPAQQ YDYVPGAVVL SKVQGYNATA TGNVGRFYIK
SFGGNRNNDE PSENKVVAFD QPTLCHPGTW YIVEADFQKM LAALLKRCDH AIEDVVPNEE
GQHTQVAIQQ LQKDLAPARD LVAKQAAVSQ EVYETYVKAY EKFLAAPKTT AVEALTSNHY
YVIRSAHPQM TGYVAQLKDG LVVPTKVEAP VTTDENPTIL WQLIRQEDGN FVLVNKAEKK
YAVVRNASAG ESIVENSTPY AWQLRYRKTN EISGFLIMAG TSNYGWYLPS NPVATTRVSL
RIANQWNNYW KLEPTAVPTG LDRSPLFQEA TGTTYDLSGR VATPHQRGVV IDAAGHKQVR
//
