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Database: UniProt
Entry: R9GXJ1_9SPHI
LinkDB: R9GXJ1_9SPHI
Original site: R9GXJ1_9SPHI 
ID   R9GXJ1_9SPHI            Unreviewed;       231 AA.
AC   R9GXJ1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Putative glycoside hydrolase, family 43 {ECO:0000313|EMBL:EOR96205.1};
GN   ORFNames=ADIARSV_0610 {ECO:0000313|EMBL:EOR96205.1};
OS   Arcticibacter svalbardensis MN12-7.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Arcticibacter.
OX   NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR96205.1, ECO:0000313|Proteomes:UP000014174};
RN   [1] {ECO:0000313|EMBL:EOR96205.1, ECO:0000313|Proteomes:UP000014174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MN12-7 {ECO:0000313|EMBL:EOR96205.1,
RC   ECO:0000313|Proteomes:UP000014174};
RX   PubMed=23846277;
RA   Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA   Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT   Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT   Sample.";
RL   Genome Announc. 1:E00484-13(2013).
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:EOR96205.1}.
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DR   EMBL; AQPN01000022; EOR96205.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9GXJ1; -.
DR   STRING; 1150600.ADIARSV_0610; -.
DR   PATRIC; fig|1150600.3.peg.600; -.
DR   eggNOG; COG3507; Bacteria.
DR   Proteomes; UP000014174; 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   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EOR96205.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014174};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   SITE            169
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   231 AA;  25996 MW;  1E8853977FA09813 CRC64;
     MIIFGPLSLL SLQSIASNNQ INLKDTTFKS NGNPIIKHKY TADPAAIVYK DKVYIYTGND
     VAPAGKSSYV MHDWLCFSSS DLVNWTEHPI PLRVTDFKWA QDDTWASQVI ERNGKFYWYV
     AVEHGTIHVK SIGVAVSDSP TGPFKDARGS AIITNDMTKA ASISWDDIDP TVIIDDQGQA
     YLFWRNTACY YAKLKPNMIE LDGRINTIKQ VIQIRFIRPS LTLKAKVIFL S
//
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