ID I4EXP7_9ACTN Unreviewed; 520 AA.
AC I4EXP7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:CCH88160.1};
GN OrderedLocusNames=MODMU_2731 {ECO:0000313|EMBL:CCH88160.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88160.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH88160.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH88160.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; FO203431; CCH88160.1; -; Genomic_DNA.
DR RefSeq; WP_014740752.1; NC_017955.1.
DR AlphaFoldDB; I4EXP7; -.
DR STRING; 477641.MODMU_2731; -.
DR KEGG; mmar:MODMU_2731; -.
DR PATRIC; fig|477641.3.peg.2588; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_039823_0_0_11; -.
DR OMA; PWENSPH; -.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000006461; 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 CDD; cd09002; GH43_XYL-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF2; XYLOSIDASE_ARABINOSIDASE; 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:UP000006461}.
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 142
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 520 AA; 56702 MW; A2C81B95BD6EB0DA CRC64;
MGSTTRWGAG PEGRRIADLG DGTYRNPVLA GDFPDPSVLK DGEDYYLTTS SFDAAPGLLI
HHSRDLVNWA PLTFALPRPI TTGFAVDIAA HDGRYFIYIP FIPSAWAEPD FGSEARIYVI
HADSMAGPWS EPIDLGITGA IDPGHVVGED GRRYLFLSGI RRVRLTDDGL ATDGPVEHVY
DGWRYPDDCV TEAYALEGPK LFHRDGWFYL VSAVGGTAGP PTGHMVTVAR SRSVHGPWED
DPANPVVRTR SAEEAWWSRG HATVVEGPRG DWWLVYHGYE NGYRTLGRQV LLEPVEWTED
GWLRALGGDL SEPLPKPIDL PDQPAGIPLS DPLAGPALGP QWAFHAPARD ETARLQFLEG
ALRLAGKGTG PADASPLTVP TGDRAYEVEV TLERVGPGAQ GGLLLFFNSA LFLGMGWDGT
TLVTYGGGKR SHYREPVAPS DSLHLRIRND RHVVTFWHSP DGVDWTRHGM RFEASGYHAN
TAGDLLSLRP AVFAAGQDAV TFRVFRYRAL PEVDAPAGAE
//
