ID A0A168F871_9MICO Unreviewed; 475 AA.
AC A0A168F871;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Extracellular endo-alpha-(1->5)-L-arabinanase {ECO:0000313|EMBL:ANC31011.1};
DE EC=3.2.1.99 {ECO:0000313|EMBL:ANC31011.1};
GN ORFNames=I598_1455 {ECO:0000313|EMBL:ANC31011.1};
OS Isoptericola dokdonensis DS-3.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC31011.1, ECO:0000313|Proteomes:UP000076794};
RN [1] {ECO:0000313|EMBL:ANC31011.1, ECO:0000313|Proteomes:UP000076794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-3 {ECO:0000313|EMBL:ANC31011.1,
RC ECO:0000313|Proteomes:UP000076794};
RA Kwon S.-K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT dokdonensis DS-3.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP014209; ANC31011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168F871; -.
DR STRING; 1300344.I598_1455; -.
DR KEGG; ido:I598_1455; -.
DR PATRIC; fig|1300344.3.peg.1461; -.
DR OrthoDB; 9759709at2; -.
DR Proteomes; UP000076794; Chromosome.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd08998; GH43_Arb43a-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:ANC31011.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:ANC31011.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076794}.
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 44
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 239
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 172
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 475 AA; 49972 MW; EAC97F3EA13B415D CRC64;
MTELREPAAG PTGGGPGATA PVIPPTAAPD APDTTSWGGR HAHDPTVARD DDGVYWCFST
DARYDGPVRA GVQVRRSTDL VTWELTGWAL PGVPPAAAAW ASAEGLWAPE VVRSPDGGWR
MYYSASSFGS RRSAIGLATA PHPAGPWTDA GLVVSSRHHE PPEGTGHPNA IDAAVVDDDD
AQWLVYGSFF GGIHALPLDP VTGLVAERAA ASAAPGALTD HPGVLLARRS PAVDNGAVEG
AFVLPRPGGG WALLVSYDSL ASSYHVRAAV ADAVTGPYRD RTGRLMTDTD AAPWSVGVPV
LSGHRHDGGP GVLAPGHGSV LTEDLPDGGR RQTFVHHVRD ADAPARHRLQ VRRLVWTHDG
WPLVSPQPWA GAARETDDED AWPSDPAVLD GRWESWEPGA DPTHVRTTTT GVLEPRDEVR
SHGRGRFGWR APDGAEVSAV VHPGWDAVRG RATLVLTALD ATGRVVLATR VDEGA
//
