ID S4Y718_SORCE Unreviewed; 474 AA.
AC S4Y718;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Glycoside hydrolase family 43 {ECO:0008006|Google:ProtNLM};
GN ORFNames=SCE1572_39145 {ECO:0000313|EMBL:AGP39990.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP39990.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP39990.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP39990.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP003969; AGP39990.1; -; Genomic_DNA.
DR RefSeq; WP_020739706.1; NC_021658.1.
DR AlphaFoldDB; S4Y718; -.
DR STRING; 1254432.SCE1572_39145; -.
DR KEGG; scu:SCE1572_39145; -.
DR PATRIC; fig|1254432.3.peg.8866; -.
DR eggNOG; COG3940; Bacteria.
DR HOGENOM; CLU_045676_0_0_7; -.
DR Proteomes; UP000014803; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; PF04616; Glyco_hydro_43; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187}.
FT SITE 216
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 474 AA; 51799 MW; DCFFFE54349435D0 CRC64;
MDAELMHIRL QTPAGAPFAF GIAVEVRGAR GFQVAEPGQG ARRYEVAQAE QPDYLDLFET
LARDFGTRVP LARTPPPPRN GGPPLRPLLT EAVALEILYG YGDPCVARVG EGEWRLLVTS
NDAPNAFPIL ASSDLFAWRL TGFVFPEGHA PAWALTGPGR ADFWAPEMHR VGEETWLCFT
ARMRDRSLAI GLARSRSPDG PFSADEAPIV TGDVIDGHIL VDARGAPWLV WKKDDNGVWP
RKLAALLHRE PAWVSELFAA PEDQRTAVLA LTLWPWAETR EPMEQFFVLQ PLIEAATADF
AGFARRLEGL RGRACGARAE EIAAISRALR TRIYARRLSA DGRSLEGEPA VILENDQPWE
AHLIEGVWIT QQGGRYHLLY AGNDFSTAHY GIGAAVAEAP AGPYRKSPEM LLSSSAEWWG
PGHPSVAVGS DGRHHIFLHA FRPGVAGYKA FRALLAAPIR FEGGVVSVDG STTR
//
