ID F3QPN9_9BACT Unreviewed; 461 AA.
AC F3QPN9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=F5/8 type C domain protein {ECO:0000313|EMBL:EGG58233.1};
GN ORFNames=HMPREF9442_00126 {ECO:0000313|EMBL:EGG58233.1};
OS Paraprevotella xylaniphila YIT 11841.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Paraprevotella.
OX NCBI_TaxID=762982 {ECO:0000313|EMBL:EGG58233.1, ECO:0000313|Proteomes:UP000005546};
RN [1] {ECO:0000313|EMBL:EGG58233.1, ECO:0000313|Proteomes:UP000005546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11841 {ECO:0000313|EMBL:EGG58233.1,
RC ECO:0000313|Proteomes:UP000005546};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:EGG58233.1}.
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DR EMBL; AFBR01000001; EGG58233.1; -; Genomic_DNA.
DR RefSeq; WP_008624112.1; NZ_GL883805.1.
DR AlphaFoldDB; F3QPN9; -.
DR STRING; 762982.HMPREF9442_00126; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_4_10; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000005546; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18608; GH43_F5-8_typeC-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..461
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003305301"
FT DOMAIN 363..461
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 158
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 461 AA; 52271 MW; 7648AFF88F0D6025 CRC64;
MKMKWKRIMA LGQAFSVVAI MDAQVVNPFG NALVPDMIAD ASIQEIDGMF YCYATTDGYG
RGLETSGPPV VWKSRDFVHW SFDGTYFPSA ATEKYWAPSK VVQANGKYYI YPTVNGYMYP
AVADHPEGPF KLARGEDRFY KPYTASTLLQ TKDPGGIDAE VFIDDDGQAY VFWGRRHVAK
LAKDMITVDS VVHVISTPRK EYSEGPIFFK RKGIYYYLYT IGGDEKYQYA YVMSKVSPLG
PYEYPEQDIV STTDYEQGVF GPGHGCVFNT DGDHYYFAYL EFGRRSTNRQ TYVNRLEFNE
DGTIRPVKLS LDGVGALRKV KGRKEIKADT VYASSTAAPM FIKPMKDEAC RRTEYFVPAF
AADGANGSRW MAAEGDKDKW LVADLGRIRK IRCSEIYFVR PTAGHAYQLE GSVDGTTWRK
CGGHDDLRVK SPHVDEPKGK YRFLRVRIKE GIAGIWEWNI Y
//
