ID A0A163LMH2_DIDRA Unreviewed; 1569 AA.
AC A0A163LMH2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Exo-1,4-beta-D-glucosaminidase {ECO:0000313|EMBL:KZM27927.1};
GN ORFNames=ST47_g928 {ECO:0000313|EMBL:KZM27927.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM27927.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM27927.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM27927.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:KZM27927.1}.
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DR EMBL; JYNV01000042; KZM27927.1; -; Genomic_DNA.
DR STRING; 5454.A0A163LMH2; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0052761; F:exo-1,4-beta-D-glucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05352; MDH-like_SDR_c; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR043534; EBDG/EBM.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041351; Ig_GlcNase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43536; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43536:SF1; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF18368; Ig_GlcNase; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 310..429
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 436..531
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 560..661
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 883..995
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 1450..1548
FT /note="Exo-beta-D-glucosaminidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF18368"
SQ SEQUENCE 1569 AA; 173672 MW; 21E9FB39A94C2F9A CRC64;
MVPIPQANEL KDLFSLKGKV VIVTGASGPT GIGIEAARGC AEYGADLAIT YNSRADGAEK
NAKELSEKYG VKVKAYKCQV GVYSQCEQLV QDVIKEFGKV DVFIANAGKT ADNGILDATV
EQWNEVIETD LTGTFNCARA VGLHFRERKT GSLVITASMS GHIANFPQEQ TSYNVAKAGC
IHLARSLANE WRDFARVNSI SPGYIDTGLS DFVPEDIQKL WHSMIPMGRD AKAKELKGAY
VYFASDASSY CTGSDLLIDG GYCASMSFPP AKPALAPSVK QPAKKENFGN LGPWAEPSWY
SSLASPYYNE SHKRLRNALR SYIDDNVKPF MLEWEAKGEA PVEECRKWAR TGFAFGDVPE
QYRPKDVPGP AGIPVGELDV FHLLISTDEG SRIEGGVGTA LGGGSVIGVP PIVHHGTEEQ
KQKWLPGLFN WETSFCLGIT EPSGGSDVAN IQTTAKKTPD GKRYVVNGYK KWITGIPTAT
HMTTAVRTGG SGMGGISVIV IPVDSKGFTW RRIPNSGQNG GGASFVELDD VQVPVENLLG
KENEGFRIIM TNFNKERFII HKLATVGRYV ESHWAWLEQL AYHIQQSPLG WQDSEIAGQI
ALSKVHGGRI LEMANREAQQ IFGGAGYQKG GPGAIIEQMS RDLRMMVVGG GSEEIIADLA
VRQETALAKR RGWRLINLQW SSRLLWAATS LASLPATTAS SLSTTTIASW KVASTRDVGI
NTAKLSAPDL DTSSWYTIDS KGTLMSTLLD NGVYNDTSLF FSENLQDVDI RQFRVAWFYR
AEFEHQEEND TLTQLITNGI SSRADFWLNK EYFSETTGAY GGAELDITSK LRLGTNILLV
KVYPTDYNRD FALGFVDWNP YPPDNGTGIW RDIQLKKTGQ VSLDKPRIKT TLEGDVDFSV
SVKNLGEKRI EGRVQCAVTD PDGKELGRPR VSFGADGKAS DLVALYLKVK TPQTWYPSQW
GDQPLYSVQC TATKNIASDV SSVYDQTSKT RFGIRTVTSR LNPYNDTVFS VNGHPFQVLG
AGYTSDIFLR FDLEKLRAHF QYVLDMGMNT VRLEGKQEHP ELYDLADEMG IMLLPGWECC
DKWEGWTYNE EGTGEKWDNK DYETAARSMA HEASMMQNHP SVMGFLVGSD FWPDNRATDL
YVNTLRDYNW TTPIIASASQ NGFPSRLGNG GLKMTGPYDW VPPNYWYDTD NGNNTHLGAA
FGFGSELGAG VGTPEYGSLT KFLSSSDLDD LWKSPDKGLY HMSTNVSSFY TRTIYNEGLF
KRYGSPKSLA DYIFKSQMAD YEATRAQFEA YLSRWSAERP ATGLVYWMLN NAWPSLHWSL
FDYYLHPGGS YFGTQSALGN MESAVYDYHS RDIYLVNRNL FPNDANSTRS VDVSLISLSG
ETIAEETSNA LTTPNTSNRA TRIEALDNIT EAVLLRLILR SSSSDNDILS RNVYWLAPNP
DILDWDNSTW YHTPVTSFSN LTALETMDEA TIVVRGKGQS IQLENTSDVP AVFVRLNLVD
EQDRDVVPVL WETNYITLWP RESYDIAVSA GSGLAVDELR VQIDGRNVRS RTVRLNGGTQ
VLEGDGFQL
//
