ID A0A178AX56_9PLEO Unreviewed; 641 AA.
AC A0A178AX56;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Endo-1,5-alpha-L-arabinanase A {ECO:0000256|ARBA:ARBA00042202};
GN ORFNames=IQ06DRAFT_131770 {ECO:0000313|EMBL:OAL02131.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL02131.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL02131.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL02131.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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}.
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DR EMBL; KV441710; OAL02131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AX56; -.
DR STRING; 765868.A0A178AX56; -.
DR InParanoid; A0A178AX56; -.
DR OrthoDB; 2719402at2759; -.
DR Proteomes; UP000077206; 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; cd08983; GH43_Bt3655-like; 1.
DR CDD; cd18828; GH43_BT3675-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; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 520
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 470
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 641 AA; 70859 MW; B44558E9DCBD1CA0 CRC64;
MQLDPFEGYA FAYFTGNSRD GENIFLAASE GNNALSWTEL NNKQPILTSS QGTKGLRDPF
VIRSHEGDKF FLLATDLSIG SGTSWGDAVR KGSLYLEIWE SSDLKTWSQQ RHVQVSPPTA
GNTWAPEAYY DDELGEYIVF WASSLYEESD TDHTGATYHR MLYVTTRDFV TFSEPVVWQD
AGMSRIDSTV LKEGDTYYRF TKDEGASGTG CSDIIQERSS SLRATLDSWT QVTACIGKNA
GTSAVEGPTV FKANPNDVNG EKFYLFVDEY GGRGYIPLET ADIANPSWKV PASFKLPASP
RHGTVIPITA KELANLRGTT ASAKRTESPK NSIVARDSPV LKGLYADPNI AIFGSKYYIY
ATTDGFPGWS GKVFYSWSSP DLVQWTRSNE PFLTLNGTSG NVPWATGDAW APTIISRNNK
YYFYFSGQNP TYNRKTIGVA VADSPEGPFV AQPQPFILNN EAVTTGQAID SAAFRDPTTD
TYYLFWGNGE PPLYAELSDD MLSLKPNTIK AISGLTDFRE ALFVNYREGI FHLTYSIDDT
RSENYRVGYA TSSSVHGPWT YRGIVLQKDV SKGILGSAHS SIVNVPCTDD WYIAYHRFAI
PNGNGTNRET TVDRVYFDDQ GIMKPVVPTL ESVAPQTIGT C
//