ID K6ZF58_9ALTE Unreviewed; 550 AA.
AC K6ZF58;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glycoside hydrolase family 43 {ECO:0000313|EMBL:GAC22045.1};
GN ORFNames=GARC_5110 {ECO:0000313|EMBL:GAC22045.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC22045.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC22045.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC22045.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC22045.1}.
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DR EMBL; BAEO01000067; GAC22045.1; -; Genomic_DNA.
DR RefSeq; WP_007625612.1; NZ_BAEO01000067.1.
DR AlphaFoldDB; K6ZF58; -.
DR STRING; 493475.GARC_5110; -.
DR eggNOG; COG3507; Bacteria.
DR Proteomes; UP000006327; 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; cd09001; GH43_FsAxh1-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:SF13; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00930)-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:UP000006327}.
FT DOMAIN 349..544
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 53
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 161
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 550 AA; 61753 MW; 740317156681F7EE CRC64;
MSAVLLLGCQ PRLNKDQENL SVATQKGISQ LLWESDLGDG NYQNPILHID YSDPDVVRVG
GGYYMTASSF NAAPGLPILH STDLVNWQLI NYALPQQVPL EVFEIPQHGN GVWAPNIRFH
DDKFWIFYPD PDFGIYVVTA TDPAKEWSKP KLILAGKGLI DPTPLWDGDG QAWLLHAWAK
SRAGFNNVLS LRQMAKDVSW VSDDYEHIID GHSLPGYRTV EGPKFYKRNG YYYIFAPAGG
VETGWKTVFR AKNIKGPYET KIVMAQESSL INGPHQGSWI HTEKNEDWFI HFQSRKAYGR
VLHLQPVKWI NDWPVIGDDA DGDGVGQPVY THLKPATDNA GKIKRQPTSD EFDLDKLGIQ
WQWNANYKED WYSLTASSGK LRLFGQPKIN TTGDNLWMTP SLLLQKNPAL TYEVITQVDL
ANSSEKAEGG LLVFGENYSW IGIKPIEGKP HLVYVSCTGA RKGCNESVHD YGPIDGATLE
LRYIMNADAT VVFSYRTDSS GRYKVIGEHF NAVRGRWVGV KVGLFSVSTT SNSGTYLDID
YIRFSPLPRR
//
