ID A0A100IDV9_ASPNG Unreviewed; 407 AA.
AC A0A100IDV9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glycosyl hydrolase family 43 protein {ECO:0000313|EMBL:GAQ39424.1};
GN ORFNames=ABL_03126 {ECO:0000313|EMBL:GAQ39424.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ39424.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ39424.1}.
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DR EMBL; BCMY01000004; GAQ39424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100IDV9; -.
DR VEuPathDB; FungiDB:An07g04930; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1164356; -.
DR VEuPathDB; FungiDB:ATCC64974_46680; -.
DR VEuPathDB; FungiDB:M747DRAFT_360320; -.
DR OMA; TWYAYAT; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd08999; GH43_ABN-like; 1.
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; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:GAQ39424.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 307
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 236
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 407 AA; 44329 MW; 6F099313B5449E07 CRC64;
MKGLPSLLNS SSTTKNWTQS TPSTDTAENE GQSGSTITPT KPPSADTPPG GSKNPMIWTR
RKITWLITLI ALSVAIIVVV ITVPVVLLVD DAHDDDPSYY NSANRPVRVV HDFPDPGLIQ
VNSTWYAYAT VATPDNPDVP HVPVSTSRNF SSWTWLQGYD VMPAMSSWET NMNQYAPDVI
QRKDGRFVLY YSGELKDWLR HHCVGAAVSN STSPLGPYIP HNSTLACPRD HGGAIDPAPF
KDVNGTLYVV YKVDGNSVGH GGDCNNGKKP IVSTPIMLQQ LNDDGVTPVG DPVEILTNEK
VDGPLVEAPD IIRTDRGIYY LFFSSHCYTS SKYSVKYAWS TSLKGPYTRA ERPLFRTGDF
GLKSPGGATA SIDGSKIVFH AFCGDYRCMF AAAMNITANY TILPAAL
//
