ID W6TV93_9SPHI Unreviewed; 686 AA.
AC W6TV93;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Sialidase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=N824_19575 {ECO:0000313|EMBL:ETZ23657.1};
OS Pedobacter sp. V48.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ23657.1, ECO:0000313|Proteomes:UP000019145};
RN [1] {ECO:0000313|EMBL:ETZ23657.1, ECO:0000313|Proteomes:UP000019145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V48 {ECO:0000313|EMBL:ETZ23657.1,
RC ECO:0000313|Proteomes:UP000019145};
RX PubMed=24578271;
RA Bitzer A.S., Garbeva P., Silby M.W.;
RT "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT Coastal Sand Dune in the Netherlands.";
RL Genome Announc. 2:e00094-e00014(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:ETZ23657.1}.
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DR EMBL; AWRU01000006; ETZ23657.1; -; Genomic_DNA.
DR AlphaFoldDB; W6TV93; -.
DR STRING; 509635.N824_19575; -.
DR PATRIC; fig|509635.5.peg.1180; -.
DR eggNOG; COG3507; Bacteria.
DR eggNOG; COG4409; Bacteria.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000019145; 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; cd08991; GH43_HoAraf43-like; 1.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR38792; BNR/ASP-BOX REPEAT DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_7G06430)-RELATED; 1.
DR PANTHER; PTHR38792:SF3; BNR_ASP-BOX REPEAT DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_7G06430)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
FT ACT_SITE 396
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 564
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 501
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 686 AA; 76634 MW; E1E9E612DDE5CB4D CRC64;
MKVAVQICTI AQFCALLSYG CGKKNETVGV PQKPSVKSHI EWDYNTLKKV SSSDAGERYC
GYARMIQLQD QSLLAIYEAD GNIVTVKSAD LGATWSAPVS VAQRANGTNM SVPDILELKD
HSLLACYNPR PYDISPSRKF GIRTKKSYDG GLTWKDEKLL YEAGYEFKNG CWEPSAVQLP
NGEIQLYFAN EGDYLNSDEQ NISMLRSSDN GKTWTEKPQI VSFRTGKRDG MPVPLLLNNG
KETVFAIEDN GFDTFKPYII RNTLKDNWAN TVDAGSPNRS YALADKIADN IYAGAPYLRQ
LKTGETILSY QGTEGRTNKM EFADMKVVIG DDQARNFNRK STPFIIPANK SCLWSSVAIL
NDNTIVAVTS TNAYSNHSEI WMIKGRLVQD PIALADPTIF LDNDKYYLYG TSSDMGFEVY
ESSDLKNWKG PVGKNKGFAL VKGESFGSKG FWAPQVFKHK NAYYMAYTAD EQIAIAKSDS
PLGPFKQEQI KSLSGIGKQI DPFVYFDTDG KTYMYHVKLK EGNRIFVSEM KPDLSDVLQE
TTKECISGVL AWENTEKTDW PVTEGPTVIK HKNLYYLIYS ANDFRNKDYA VGYATSTSPM
GPWKKYAGSP IISREKLKQN GTGHGDLFTD KSGNYKYVMH THHSATKVSP RSTGIIDVKF
ARGDEADVLQ ADESTFKLLF TDAETK
//
