ID T0K3L7_COLGC Unreviewed; 1045 AA.
AC T0K3L7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Endo-1,5-alpha-L-arabinanase A {ECO:0000256|ARBA:ARBA00042202};
GN ORFNames=CGLO_14594 {ECO:0000313|EMBL:EQB46354.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB46354.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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}.
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:EQB46354.1}.
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DR EMBL; AMYD01003426; EQB46354.1; -; Genomic_DNA.
DR AlphaFoldDB; T0K3L7; -.
DR STRING; 1237896.T0K3L7; -.
DR eggNOG; ENOG502SM7B; Eukaryota.
DR HOGENOM; CLU_010779_2_0_1; -.
DR OMA; MWSEDDT; -.
DR OrthoDB; 2719402at2759; -.
DR Proteomes; UP000015530; 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 Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.2340; -; 1.
DR InterPro; IPR046780; aBig_2.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; PF20578; aBig_2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 2.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EQB46354.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1045
FT /note="Endo-1,5-alpha-L-arabinanase A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004565743"
FT DOMAIN 27..105
FT /note="Atrophied bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF20578"
FT ACT_SITE 741
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 913
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 864
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 1045 AA; 113318 MW; 4A8B827392C54A6F CRC64;
MPSFRLWLSS ALAFAATVRG QDATEQVEAA LAALTVTNVD DVRGNLYLPT AINGINITWA
SNASSIISDD GVVKRQTEDA QVALTATIEY DGVSQQKDFV ASVRKAVVLD PFEGYAFSYF
TGSTIAGENI FFAASQGNDA LDWTELNSGQ PTLTSSYGTK GLRDPFLIRS HEGDTFYLIA
TDLSIGSGTS WGDSVRIGSR YLEVWQSNDL INWSAQRHVL VSPPEAGNTW APEAYYDEDL
GAYLVFWASS LYEDSDVNRT GSTYHRMLYA TTRDFVTFSD TQIWQDAGMS RIDSTVIKSD
GTYYRFTKDE GASGTGCSDI IQESSTSLRA TLDSWTIIDS CIGKKAGTSA VEGPTSFKSN
PGDVHGEKFY LFVDEYGGRG YIPLETTDIG NPDWTVSSSY NLPSSPRHGT VIPVTASELA
ALTGTTTTRR DVSADGEILR YDFSSVDGTT VQDVSGNGNN AVINGGATIT DGALTFDGVD
DYVKLPDNII AGVTNIAIEA KVLVDASQQT PYFIYGLGNT VSGSGNGYLF STGNPYRASI
TTGNWTGEKT SSSGSQLPSG TWLHLVFTQQ GRTTVIYLNG YEVARNEDVN INPSNIGNGV
TTANYIGRSL YDSDKLFKGH VKEFAIFNRS LSAAEVLSRS GNVGAITEVA LADSTAQKVP
PIINTTDNKV LFPVYPGTDL ANLAPVFTTT EGVTSSPASG TPVDLTSEVK YVLTKGDEVV
AAWEIKAVEM GSPVLPGLYA DPNIAVFNGE YYLYVTTDGV PGWGGNKFYV WKSSDLVTWT
RSEDPFLVLD GANGNVPWAN GNAWAPTIAE RDGKYYFYFS GNNIALNTKT IGVAVADSPE
GPFTAEPDAM ILNNEAITAS QAIDPAAFQD PVSGKYYIYW GNGRPLVAEL NDDMVSVKWD
TLQAMTGLVD FREGLFVVYR QGLYHLTYSI DDTGSENYRV GYATSENLSG PWQYQSVILQ
KDTSQGILGT GHNSMFNVPG TDDWYIAYHR FQIPGGGGYM RETTIDHVYF DENTGLIKPV
VPTLTSVEPQ TVPQKIRRRS RIMRL
//
