ID A0A0Q5TZA0_9SPHI Unreviewed; 434 AA.
AC A0A0Q5TZA0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=F5/8 type C domain-containing protein {ECO:0000259|PROSITE:PS50022};
GN ORFNames=ASG14_07055 {ECO:0000313|EMBL:KQS36789.1};
OS Pedobacter sp. Leaf194.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1736297 {ECO:0000313|EMBL:KQS36789.1, ECO:0000313|Proteomes:UP000051708};
RN [1] {ECO:0000313|EMBL:KQS36789.1, ECO:0000313|Proteomes:UP000051708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS36789.1,
RC ECO:0000313|Proteomes:UP000051708};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS36789.1, ECO:0000313|Proteomes:UP000051708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS36789.1,
RC ECO:0000313|Proteomes:UP000051708};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQS36789.1}.
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DR EMBL; LMPU01000008; KQS36789.1; -; Genomic_DNA.
DR RefSeq; WP_056870597.1; NZ_LMPU01000008.1.
DR AlphaFoldDB; A0A0Q5TZA0; -.
DR STRING; 1736297.ASG14_07055; -.
DR OrthoDB; 9803461at2; -.
DR Proteomes; UP000051708; 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; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..434
FT /note="F5/8 type C domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006263830"
FT DOMAIN 292..433
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT ACT_SITE 30
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 129
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 434 AA; 49626 MW; D8EF602B24FB2DC7 CRC64;
MKTLYLLLSL LSIAFFGYSQ NPVIPGYYAD PSIKKFNGKY YLYVTTDGYG EFGNDGQTLV
WVSDDLVVWK AEKVEGLPNE TVWAPAVSKG KDGKYYLYRQ NSVDYSGYAY KGDTPTGPFK
QMNHIGGFDL EPFIDPVSGK TFVISASKEL FEMNNDLKSP DYLVKVEKKI PLKGTLFDFT
EAPYMLHKDG LYYLMWAGGR CWQRSYNIKY AVSKNIDGPY TSIDNGIVLA TNEAEGILGP
GHNSVIELNG RWFIFYHRQD PDSSNPCSFR FTCMSEITFD RNGKIQLTQL INDLPKTLGI
KPKMINFALN AETFANTERL THRAMYAVDG KNDTRWTTEV NQKGQLSINL GAERQIKQIE
IDFEYPDKWH TFKLEYSKDN QNWTTIADHT QQAVQAYPNM FNEVDIKANF IRLSINNSED
RTASVWEIKV WGNP
//
