ID B0N7I5_9FIRM Unreviewed; 1718 AA.
AC B0N7I5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Hyalurononglucosaminidase {ECO:0000313|EMBL:EDS17773.1};
DE EC=3.2.1.35 {ECO:0000313|EMBL:EDS17773.1};
GN Name=nagH {ECO:0000313|EMBL:EDS17773.1};
GN ORFNames=CLORAM_02568 {ECO:0000313|EMBL:EDS17773.1};
OS Thomasclavelia ramosa DSM 1402.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=445974 {ECO:0000313|EMBL:EDS17773.1, ECO:0000313|Proteomes:UP000005798};
RN [1] {ECO:0000313|EMBL:EDS17773.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS17773.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium ramosum(DSM 1402).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS17773.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS17773.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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:EDS17773.1}.
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DR EMBL; ABFX02000008; EDS17773.1; -; Genomic_DNA.
DR RefSeq; WP_003538439.1; NZ_DS499659.1.
DR eggNOG; COG1196; Bacteria.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_001501_1_1_9; -.
DR Proteomes; UP000005798; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 1.20.1270.90; AF1782-like; 3.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 1.20.58.460; Hyaluronidase post-catalytic domain-like; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
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; PF00754; F5_F8_type_C; 3.
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; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF140657; Hyaluronidase post-catalytic domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 2.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EDS17773.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDS17773.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005798};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1694..1713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 633..763
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 774..930
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1718 AA; 190654 MW; 63918497B2873298 CRC64;
MARFWDKALK SSLAMLVVFS TLFFMSPNIK VEAKETNYEI YPTPHEITYQ DKDYVIRSQV
NVVYEDGIDA ATKKRMTEVL ESKNKQISTS KQKVDGKTNI LVGTYKSGGY VDGYVKSNYS
VEESLFSKFG AHFVASNNGE IVILGKDTDG AFYGITSLKH IFNQMDGSTI RNFVIKDYAD
TDIRGFIEGY YGIPWSNEDR MSLMKFGGDF KMTSYVFAPK DDPYHKNLWR ELYPEEELAA
IKEMVQVGND SKCRFVWTAH PFMGGFNASK VDEEIASLLK KFDQLYDAGV RQFGVLGDDV
GSLDRSVVIK MMNSVSAWAK EKGDVYDSVF CPAGYNHSWQ GDYSELSDYD AGFPEDVKIF
WTGEAVCQPV EQKTLDHFKR NRLPEGADER RSPLFWLNWP VNDINGSRLM MGKGSLLHTD
INIDDLSGVV TNPMQEAEAS KVAIFAVADY AWNVKSFNDD QSWADSFKYI DQEASEELHT
LAKHMSNPQP NGHGLVLAES EELQPLINEF KTKLANGDSI IESGKQLIAE MNVIIDACDG
FHANSKNENL KKELLSFTGS LKDLTTAIKH FTESAIAIEE NDMVTAFNQF SNASSELINS
QNHIRKLLNG TAKVSPGSTH LIPLAKALQD KLSGPINDYI ASGETEQPLE ISASSSFTTW
HSGKIADIVD GNNDTAAWHN GYEKAGQYFQ VDLSKPTTIY GVHILNGANN SDKKEDTFGY
AKLQYSTDGT TFKDLNKEVY GEYASQVDVT NIEIEDVVAV RYVCSEVGGG NKWPAMREFT
VVTQPAEEEQ FTKEVIRTTD GWSIYGGSDA NLIDGDLTTK VHYNVRQKGE PANTTIPGDY
VGVKLSKPIT LGKINILQGN TDSDGDYFKD ADLQYSLDGK TWTTVETYKN TINIVTDLSD
QNITAQYVRL VNKVNQNTWI AMREFDVAAK VYHNGKVFTN VSEYKSLTAD YLDESAKITP
AKGITLANGD YVGLKLDRIH ELKDIVSELT NDSLTIQVSK NSYEWQNVNA GNVSADARYV
RIINNNEAEV TFDLNKFIVN TVEIKEKSIT SSNFSIDKPL NVFDGDLTTA TAYQGSQNVG
KYFTYDLGQE ITLNSFKAIC TDSEWDYPRH GKFSVSTDGE TWTEIMLLGN QNENNPGEAE
NTDEIGFVLP SHEISYNAKK VDGLNLQARY LKFEITRTKV GADKWVRFQE LEINNGEFIP
SQNNPTFTSS SQETRDGLFS YMVDGDISTM FIPKDANGYV NYSLSSNNQV NTIKIIQNSA
VISNAVVKAR LFTNASAEQW VTLGTLSQAI NEFVLPENTI LLDIKVEWGD VIPNITELST
YKSEVTTLNV DALKALIDNK EDLSSWTAAA AATYGDAYNA GKQVLESEYA SQTTVDNAVR
AINKAIENKV LKGDLSKLEI IIANAHTDQN NYTAPSWLAY SKAIEAINKS IANGDNTSVA
DVDKLIANYD LANTNLVFNP SNQEEAIITI EGENDFVASV TNPEKLYTIN SWKMYLEAKA
KVEQLIIDNQ STPVHPDEFA KAISELAAAK EKLVVVGDLK DILDTANKVN QELYTTSSYK
GLADAIAEAT ARLENGTAEE IDASIKALDN ALKALVVRAK ADEVKEYINS ITLVDLSKYT
ESSAKIYQEA YNVLKAMLDN LSDISAKEFI EAKNNFETAV AKLEEKATVA PIPTPTPNEL
PASDSAKTGD DVNIFAYVTG LGVVAIVGIY WLLRKKEE
//
