ID A0A098QUZ4_9SPIO Unreviewed; 568 AA.
AC A0A098QUZ4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:KGE71233.1};
GN ORFNames=DC28_12320 {ECO:0000313|EMBL:KGE71233.1};
OS Spirochaeta lutea.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE71233.1, ECO:0000313|Proteomes:UP000029692};
RN [1] {ECO:0000313|EMBL:KGE71233.1, ECO:0000313|Proteomes:UP000029692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC230 {ECO:0000313|EMBL:KGE71233.1,
RC ECO:0000313|Proteomes:UP000029692};
RA Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.;
RT "De novo Genome Sequence of Spirocheata sp.";
RL Submitted (MAY-2014) 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:KGE71233.1}.
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DR EMBL; JNUP01000067; KGE71233.1; -; Genomic_DNA.
DR RefSeq; WP_037548948.1; NZ_JNUP01000067.1.
DR AlphaFoldDB; A0A098QUZ4; -.
DR STRING; 1480694.DC28_12320; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000029692; 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:InterPro.
DR CDD; cd09000; GH43_SXA-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000029692}.
FT DOMAIN 366..563
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT REGION 319..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 15
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 194
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 135
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 568 AA; 64523 MW; C5CE1A257D386865 CRC64;
MPTIHNPILR GFNPDPSICR VGEDFYIAVS TFQWFPGVLV YHSRNLETWT LASRPLQRRS
QLDMAGNPSS GGIWAPCLTH AEGQFWLIYT DVKNWAGSPP DHGNGFKDTH NYLVTAPDIQ
GPWSEPIYLN SSGFDPSLFH DEDGKKYLLN QVWDYRPGHN SFAGIVLQEY DHRRRRLVGP
RSNIFSGTSI GVTEAPHLYK RGDYYYLMTA EGGTEYAHAV TLARSKSLTG PYELHPQTPL
LSSVRDRQGF REARKEARDE TPFLFPGLQK AGHGSMVPWQ GDEWILAHLC GRPLPGTQHC
PLGRETALQR LTWREDAWPW PDEPGSRTTV EFSQRPGLAN TAKKSTRQPG IYQPDGVQIH
PRIWQEDFNA PGWSKELQTL RIPADDRYDI RSRPGWLRLT GAESPTSRFR QSLLARRAQS
FRWRGETKLS AVPEDFQQFA GLVVRYDEAT QYILRIQGDG QGGQSLGIIV FDQQRINLPL
AEQEVPVDGS QLWLAVRMDY RTLQFEWSQD GSAWQTIGPE LDASKLSDEY AHPMGFTGTF
LGLGCFDLSG RSFTADFDYL TYQEEDHD
//
