ID A0A0G2JAI0_9EURO Unreviewed; 328 AA.
AC A0A0G2JAI0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Endo-arabinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EMCG_08415 {ECO:0000313|EMBL:KKZ65766.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ65766.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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:KKZ65766.1}.
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DR EMBL; LCZI01000575; KKZ65766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2JAI0; -.
DR VEuPathDB; FungiDB:EMCG_08415; -.
DR Proteomes; UP000034164; 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; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..328
FT /note="Endo-arabinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002545827"
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 160
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 328 AA; 35776 MW; 18EB548EAF29A5CA CRC64;
MHQLLQSFSS LLYLAYFINA VDVNPPQLRF SEPGPHQVIP KDFPDPGFLK VSADWYAFST
NAYNKKVQVA KSSDFENWTV LNTDALAGLG PWESPLDHWA PDIIMRDDGR LVLYYSGRLK
ESPRYHCVAA AVSEGQDPAG PYHPLEEPFA CHMEKGGSID PAGFLDKDAS RWLVYKVDGN
NIGNGGDCGN SIPPLAPTPI YLQKVAGDAV TKIGDPITIL DRDESDGPLI EAPSLILSSE
GVYFLFYSSH CWTAPAYDVR YATSRSITGP YLKAAEPLIK SGDYGLKAPG GATVANNGER
MLFHANCPAG RCMYAANIEI KGETARIV
//
