ID A6NZQ9_9FIRM Unreviewed; 786 AA.
AC A6NZQ9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Glycosyl hydrolase family 2, sugar binding domain protein {ECO:0000313|EMBL:EDM98412.1};
GN ORFNames=BACCAP_03713 {ECO:0000313|EMBL:EDM98412.1};
OS Pseudoflavonifractor capillosus ATCC 29799.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoflavonifractor.
OX NCBI_TaxID=411467 {ECO:0000313|EMBL:EDM98412.1, ECO:0000313|Proteomes:UP000003639};
RN [1] {ECO:0000313|EMBL:EDM98412.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM98412.1,
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:EDM98412.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM98412.1,
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 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:EDM98412.1}.
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DR EMBL; AAXG02000034; EDM98412.1; -; Genomic_DNA.
DR AlphaFoldDB; A6NZQ9; -.
DR STRING; 411467.BACCAP_03713; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR eggNOG; COG3250; Bacteria.
DR Proteomes; UP000003639; Unassembled WGS sequence.
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; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDM98412.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000003639}.
FT DOMAIN 41..133
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 234..412
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 609..665
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 680..770
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 786 AA; 86780 MW; CDB663165DC8C7CC CRC64;
MGEEDKSIAV TLPHDAMLSE PRTAQSAGGT NTGWFEGYDY VYQKAFNVPA EWADRAMFLE
FEGVYRDAEV FVNDSKAAFQ PGGYTGFFVA LDGLLRTDSE NHIRVISRNA DQPNSRWYSG
AGIYRPVWLH VLPKEHIALN GLKIQTLHHV RPSVRVALSL ICPGTAQVSI LDGDRELAQA
ACKCQPGGTV DIPLPGAELW SPDTPKCYTC RVVFGEDVRE ESFGIRTITC DSKNGFCING
ERVILRGACI HHDNGILGAI TLPDAEMRKV RLLKQAGYNA IRSAHNPCSK ALLDACDTLG
MLVLDEYTDM WYIHKTRYDY AQYMPERWRE DLSALVDKDF NHPSVVMYSI GNEVSETAQK
RGIELTGQMT ECLHQLDNRP VTCGINIFFN FLSSMGFGVY SDKKAEQEAA KAERRKGAPA
KKKAVGSEFF NNLAGLFGSE FMKFGATLHG SDVKTRDAFA KLDVAGYNYG EKRYVRDLKK
YPDRVILGSE TFCADAARFW DLAKKHPALI GDFVWTGMDY LGEVGLGAME YRDYAPDFDH
GPGWITASAG VLDLTGASTG QTAYTQVAFE LCPIRIGVVP ADHAFEPHSP SAWRMSNTYE
SWAWNGCEGK ETRVEVYARG AKVALFLNGR PMGEKKPDRD SRAVFRVTWQ PGELTAVVYG
ADGAELGRTS LSSAGEETRL AAEPEEPRVS AEGLCYVRLR YTDENGLLKP LARGDIRVAV
EGGRLLALGS ACPYNERGYL TDTTDTYYGQ ALAIVKPKGP GELVLRAESP YGSAQVHISC
REEGAR
//