ID R7LH91_9BACT Unreviewed; 1286 AA.
AC R7LH91;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=BN805_02025 {ECO:0000313|EMBL:CDE87381.1};
OS Prevotella sp. CAG:891.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262937 {ECO:0000313|EMBL:CDE87381.1, ECO:0000313|Proteomes:UP000018147};
RN [1] {ECO:0000313|EMBL:CDE87381.1, ECO:0000313|Proteomes:UP000018147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:891 {ECO:0000313|Proteomes:UP000018147};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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:CDE87381.1}.
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DR EMBL; CBJT010000193; CDE87381.1; -; Genomic_DNA.
DR Proteomes; UP000018147; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 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 InterPro; IPR009459; MucBP_dom.
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 Pfam; PF06458; MucBP; 2.
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:CDE87381.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018147};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1286
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004451508"
FT DOMAIN 26..159
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 163..512
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT DOMAIN 959..1020
FT /note="MucBP"
FT /evidence="ECO:0000259|Pfam:PF06458"
FT DOMAIN 1179..1238
FT /note="MucBP"
FT /evidence="ECO:0000259|Pfam:PF06458"
FT ACT_SITE 342
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 1286 AA; 143522 MW; 847CF8A69D287675 CRC64;
MKQKFLSFLF LLLALPLSLS AQRFVNLTPK AKSMTVMSGN VVLPADMKVS YSADLPADMQ
HEVERFVAAF NKATGYQAQA VEADEQAMFQ VRMSKNSNMK PNGYYLLAEN NSVTVQAKSA
EGLFYALQTV KKILPPNVMA GVKDAKVTEY VLPQVQISDE PRFEYRGFML DVSRHFFTTD
EVKRMLDVMA YYKMNRFHWH LSDDQGWRVE IKKYPKLTTI GATAPNSFFT DMESCTQYWI
NKPYGPYFYT QEEIKDVVAY AKERHIEIIP EIDMPGHFVA AMAAYPEYSC TPNNPPTIWT
TGGISSNVLN VANPQAVQFA KDILSELIEL FPYETIHIGG DECPTTQWEH NELCKARYKE
LKLTNYRQLQ SHFIKEMADF VQSKGKKLAV WNESITAAGA DLNLIKQTDA LVYCWQPARQ
SAVKAKELGL KNIYTPWGPY YINRRQGNSP QDPPGAGYGT DDVKATYNEA IPSETDHGVQ
GTFWCEHVHE RNYLEWLALP RLIAIAEAGW TQQARRSFAD FQKRMSADTT LLNYGNYRYC
KYHMLDAETG GGQQTDTVMP HANKDGKNYY YRLVSGCTDN ARVGRCMELV AEGSSLITDN
GAKVGMLWTN TQAAKEAANY NYQWWSLEED PAHKDMYALV CKAQPEGSVN PNPTANNNTA
RWTYDNSQKH YNFVLATGAY GQLANGHYYY SITSNRAPEG WYMNSAAGGQ KLSVNLYNKP
DDGNSGMWQF APMENYDGPA DKPVAYTPFT VGQTVVMVNA VEGYDSTRIV DNNLGSNLRH
TLVPFSNDAW TVTEADAEVA ADGTQHVKLQ NVATKRFIGT AGTFVGGLGR PVSVGNTATE
LTVKFMTNNE FRVMHSNASF YPLPAGTVYA GSNVNGATYD APRVQGAVWK LMPVKVVTLN
CRDTEGADLG AYSLSVPTER TEALTAADCP QLKNMIVTEV KSEGDNAYTV TYKRTAYTVM
LKAVDTAGVT IQLNETAVNV GDKFTFNAPE VNYYKFESSP ITDGTEMTIA NDTTIEVVYT
TDAYTGVKEV GEAVTDVKHL KNGHCYLVYD ASDADNGARK GYRRVVADTK QVNRFTSESQ
LDPSAVWTLE GEGNKFKVKN AYYDLYIPLL QRSACPAVSK LGDTFTFTLN ADGESFKIAG
TNGMMWDGNE NGNMVGWDKG NGHPMKLYHF TAQPFFMLTL NCVTADGEKL QTVANLHAAG
ERYPLIIPVI RGYKLKGIEG NENYNDIIEQ HYTMTVTYEP IVDGIDKVTT DTPVRHQGIY
DLQGRRLQNI TQPGIYIVNG KKVLVK
//
