ID A0A177DPN4_ALTAL Unreviewed; 329 AA.
AC A0A177DPN4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU368117};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU368117};
GN ORFNames=AA0117_g16 {ECO:0000313|EMBL:RYN83922.1}, CC77DRAFT_752970
GN {ECO:0000313|EMBL:OAG21884.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG21884.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG21884.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG21884.1,
RC ECO:0000313|Proteomes:UP000077248};
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.
RN [2] {ECO:0000313|Proteomes:UP000291422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL bioRxiv 0:0-0(2019).
RN [3] {ECO:0000313|EMBL:RYN83922.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN83922.1};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL J. ISSAAS 0:0-0(2019).
CC -!- FUNCTION: Alpha-L-arabinofuranosidase involved in the hydrolysis of
CC xylan, a major structural heterogeneous polysaccharide found in plant
CC biomass representing the second most abundant polysaccharide in the
CC biosphere, after cellulose. Releases L-arabinose from arabinoxylan.
CC {ECO:0000256|ARBA:ARBA00025637, ECO:0000256|RuleBase:RU368117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000256|ARBA:ARBA00001462,
CC ECO:0000256|RuleBase:RU368117};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU368117}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 62 family.
CC {ECO:0000256|ARBA:ARBA00007396, ECO:0000256|RuleBase:RU368117}.
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DR EMBL; KV441475; OAG21884.1; -; Genomic_DNA.
DR EMBL; PDXD01000001; RYN83922.1; -; Genomic_DNA.
DR RefSeq; XP_018387305.1; XM_018533099.1.
DR STRING; 5599.A0A177DPN4; -.
DR GeneID; 29118693; -.
DR KEGG; aalt:CC77DRAFT_752970; -.
DR VEuPathDB; FungiDB:CC77DRAFT_752970; -.
DR OMA; AYQWGSS; -.
DR OrthoDB; 1772551at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR Proteomes; UP000291422; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd08987; GH62; 1.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR PANTHER; PTHR40631:SF1; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycosidase {ECO:0000256|RuleBase:RU368117};
KW Hydrolase {ECO:0000256|RuleBase:RU368117, ECO:0000313|EMBL:OAG21884.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368117};
KW Signal {ECO:0000256|RuleBase:RU368117, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..329
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040569722"
SQ SEQUENCE 329 AA; 35284 MW; BFF733EC61117503 CRC64;
MRFTPTDLSL PAAAIAFLAS TASAQSCQLP TSYKWTSSNA LAQPKAGWAN LKDFTTQMVN
GKHLVYATNH DTGSNYGSMN FGLVSNFNEL ASAPQNAMSQ GLVAPTLFFF KPKNTWVIAY
QWGATAFSYK TSSDPTNANG WSAAKPLFSG KITGSSTGPI DQTVIGDDKN MYLFFAGDNG
KIYRASMPIG NFPGDFGTAS TVVMSDSTNN LFEAVQVYTV KGGTTAKYLM IVEAVGSQGR
YFRSFTASSL GGNWTPNAAT ESNPFAGKAN SGATWTNDIS HGDLVKVTND QTMTVDPCNL
QLLYQGRNPN SGGDYDRLPY RPGLLTLKK
//
