ID A6NQW9_9FIRM Unreviewed; 973 AA.
AC A6NQW9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Glycosyl hydrolase family 3 N-terminal domain protein {ECO:0000313|EMBL:EDN01465.1};
GN ORFNames=BACCAP_00593 {ECO:0000313|EMBL:EDN01465.1};
OS Pseudoflavonifractor capillosus ATCC 29799.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoflavonifractor.
OX NCBI_TaxID=411467 {ECO:0000313|EMBL:EDN01465.1, ECO:0000313|Proteomes:UP000003639};
RN [1] {ECO:0000313|EMBL:EDN01465.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDN01465.1,
RC ECO:0000313|Proteomes:UP000003639};
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 (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDN01465.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDN01465.1,
RC ECO:0000313|Proteomes:UP000003639};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Pseudoflavonifractor capillosus ATCC 29799.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:EDN01465.1}.
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DR EMBL; AAXG02000005; EDN01465.1; -; Genomic_DNA.
DR RefSeq; WP_006571146.1; NZ_AAXG02000005.1.
DR AlphaFoldDB; A6NQW9; -.
DR STRING; 411467.BACCAP_00593; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR eggNOG; COG1472; Bacteria.
DR OrthoDB; 98455at2; -.
DR Proteomes; UP000003639; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDN01465.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000003639};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 940..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 436..510
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 973 AA; 105127 MW; 29179009D9423D68 CRC64;
MKRKGATLQR TAIAVLSILL AVSIGVTAGA TSYRTLICNA IGGEMYRLEG GDDSDTIQLY
ETNGMTLEEW KTAADQLVEE IEAEGMVLLK NEGQVLPLDS GMKLSLFSRS SVDLVLGGTG
AGGIDESKAV DLRTALEGAG FTVNPTLWEF YKGYDGKDGY TRSNGGYTGA NPEDIFVAEV
PINEYTDAVR DSYKDYNDAA VVVISRVGGE GSDMPTGDFG DGTKYLALQE QEKDLLMEIQ
ESGQFDKVIV LINSSNAMEL GWLDQEEYGI DACLWVGGVG QSGARAIAGA LAGTVNPSGR
LVDTYAADSL SAPAMQNFGD YTYTNAADVE AAGVAVGTKY VVYAEGIYVG YRYYETRYAD
SVLDPVGTNA ASSAGAFVGD TWNYTDEVCY PFGYGLSYGA EDGKPFVQEL VSAEMGEDGL
TVTVRVTNTG TAAGKDVVQL YAQQPYTAGG IEKSAIQLIG FEKTDVLEPG ASETVTITAD
KYDFASYDYK NDKTFVLDSG SYYFAVGDSA HDALNNVLAA QGKTVDDGMD YNGNAALAYT
WNNPAKELLN QSYSGNEITN RFDSADLEYY GQDVEYLTRS DWNTFPESYD SLTATDEMIY
DMNGVNNYKS SGGDLSQFQF GVDSQMTIAK MVGVPLDDDE QWDKILNQLT MEEMADIVTR
AARSPIPSIG YPAMAMNDGP QGVNRKYTED GTSATGYCGA VVRASTFNRE LIRRMGEAMG
EDWLRTDTEG AYTPAVNTHR TPYAGRNFEY YSEDGFLAGE LAYEEVMGMQ SKGAICYIKH
FALNDQETNR TGICTFSNEQ AIREIYLKAF EKSFTEGASK GTMGAFNRIG CVWAGAYAGL
MTDIVRTEWG STAIIITDIA INTAYQHIET ALAAGGNLWA TSGSSFYNWL VTAAPNDAAA
VEKMRESCKI ILYNVASSSG MNGLSPTGHV VRVTPYWETA AYAVIAVLAV LDLAAIGFMV
YGNVKARKTE VEK
//
