ID A0A1G0YXM4_9BACT Unreviewed; 966 AA.
AC A0A1G0YXM4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Beta-hexosaminidase bacterial type N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2017_13150 {ECO:0000313|EMBL:OGV50719.1};
OS Lentisphaerae bacterium GWF2_44_16.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798571 {ECO:0000313|EMBL:OGV50719.1, ECO:0000313|Proteomes:UP000176916};
RN [1] {ECO:0000313|EMBL:OGV50719.1, ECO:0000313|Proteomes:UP000176916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV50719.1}.
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DR EMBL; MHBF01000093; OGV50719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0YXM4; -.
DR STRING; 1798571.A2017_13150; -.
DR Proteomes; UP000176916; Unassembled WGS sequence.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd09620; CBM9_like_3; 1.
DR Gene3D; 2.60.40.1190; -; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR011496; O-GlcNAcase_cat.
DR PANTHER; PTHR13170; O-GLCNACASE; 1.
DR PANTHER; PTHR13170:SF16; PROTEIN O-GLCNACASE; 1.
DR Pfam; PF06452; CBM9_1; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 221..378
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 396..690
FT /note="Beta-N-acetylglucosaminidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF07555"
FT DOMAIN 800..935
FT /note="Carbohydrate-binding"
FT /evidence="ECO:0000259|Pfam:PF06452"
SQ SEQUENCE 966 AA; 110308 MW; A4CEDC80D2883F1D CRC64;
MRTGRNKWLM MSLVGILSGM LFSLEGADVK DKNMMLNGGF EELDSKNNAV SWSFGCSLPK
GKAEITTGTV YSGKNSLHLR SESINEKSDS TKTGAISASS EMLPLPPEGT KLECSVCIKL
KDVKSPGSYH KTRFTVHFFD KDRKRIKHHD LVCLDGTLDW RIFKQSLTVP SGAAFMQIAC
SLTNCTGEAW FDDVMVTVDG ESARKVTERR NSMSALPMDC PILIPEPWQI KFASYSFSVE
KVFFETPNGD SRANLALLDV LKEYNLAADK MQKDKSYDAT ALLILTGDKQ DKDLAGIFEK
DFRGRTWNEL GEQGYFLSVK EIGRKEESSV GGEMIKGGKK IVCIGANTEQ GRFYGIQTLR
QLLKAGKGKE LRAVNIVDKP TLSRRGAIVG LQWFSQRKEA IERIRQMKMN LVYHQGSFLN
LKLGCDQKTK KTFWREPFTS QELEMLREYL ELCRRNFIEV YISFAPRGLP PTCYSSDEDI
NILVGKMEAL YKVGVRNLGI SFDDLQNIEQ NKVICEADIK KFGDDFGAAH LYFVQNVYDR
LKKKCPELNF MVLPYVYGSY VNIPEKDMQY LKTLGKLSQD IKTWVVCLYT YDGVKKTPAI
AGRKPFIWDN YYTTGDLPAF PAPIDRAREL SDENITGYIF LPATPKQEDA SKISWLNAAD
YMWSPQRYNA EKSYKTAIAY VAGSAEAAEL LKEYSEFSLK IDDYKFPTEN RETRLAFLEK
TMDQLNTFDP KLKILEPKLA TAMRSDTGKY RKDLQRIIDN LKQRPYPAII YPQKGFVPTN
ENALKDFIPL SKNVKSIEAT EAWLTYDPNK LYLKVLCREP CLERLVTQRN NRDSNVFQDD
SIEIFIMPDQ ENASGDFTYY HIVINAIGTV YDAKHVHHRF NYLHEQYKDW NPELDITTSK
EKNTWILNLA IPFSALGMAS PQPGRRIFMN LCRNRMTGGK GELSCYALLL KGKYHDPWSF
WPVEFK
//
