CAZyme Information: KZZ91336.1

Basic Information

• Species: Ascosphaera apis
• Lineage: Ascomycota; Eurotiomycetes; ; Ascosphaeraceae; Ascosphaera; Ascosphaera apis
• CAZyme ID: KZZ91336.1
• CAZy Family: GH47
• CAZyme Description: AB hydrolase-1 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A167YH64]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1253	AZGZ01000014|CGC2	141268.48	6.4709

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AapisARSEF7405	6442	392613	0	6442

• Gene Location: location=AZGZ01000014:399193-404627(+)

Full Sequence      

MAVPLYAADAIEYGILCVYCVYVWLFYIATGVYSKAVFAKATQEEEKELHLARDQFWNLS
KKWQGFSHEFLTLKDGVRMHYVTNATPEMIASNRPVVIFFHGFPDSWAVWRHIITAAPLK
EGCIIVAPDLPGYGGSDSLPEYGAANLLGHVASFVIDVRKRYERPDGQDRRRSIIVAHDW
GSAIAFRLASEAPQLADRFIIANGPMNSCTLNNFREDKAKALSYLKRFRVLAAIKAAKPV
LLQILMSHYIVLFQSPIPFLRIFSTIGNYAWIRGCHKHVSGLQDGISTAELQEFMAATLG
PELKETPIATETGEKYSASVIQRGTDFALLHPMRYYREGAFTQVWEKSHELKASLDQLRS
SQLKDDEITRLGPLRAKTTVLWGMYDLALSEDICLRNLDKYLIPDSYIVELPHSGHGTPV
EAESRVVVTKVIEWAIGGEEDDVGKAISSVYPDARAMVLAHSLRDNGSSAKLAALVTADT
VSLQAIDELKTVYDDIIPIRRIVNHCPDNLFLMGRPDLYAMFSKVELWRQLQYKQLVYID
ADAIALRAPDELLEMETSFAAAPDVGWPDCFNSGMMVLRPNLDDYNAMMEMAESGTSFDG
ADQGLLNMHFKNWDRLSFTLNCTPSAHYQYVPAFRHFQNDISIVHFIGSRKPWQLPRDGG
ISGTPYQELLGHWWTVYDRHYRPKSQEELSRTQQNPQSNHTEPVSEFVESTSVKETPQMV
ASKERADKKQSAPSTAPPPYEQHQEDRKVISTDKHVEHPFSARPTGGHNEEDWIDDPQGT
HHDSTPANGPEGEPSHPYQIVEGYHPVDATDEDDTSCDVEDLYTEECRLEDPEYQEETPT
PAAYEEPPPLSIVPQYVYGEQHVRIPQVKRRPPAIKSMNQRQQGAAGTTRSASGRGRLSF
QEGIQDQPKRFMKQRAFSPHPLASRNRRVDNDARAIEQKTQTPAPREEVGRHEEQLPPWY
PPKPKFMPPMSEWNPTREPPPKRSHPEAPNLSFANYTMSKDTQLYQAPKQYFDPKPEAKK
MLQKQAPRASDRYELEDDTKRTGTTDEPTTQTTETPKPVFPWEQYEKHRASRVFSPVTSA
TMTPSESTTPATSFASRDGARPSSASSSKQFSTGDIWQCFSRQSAWDDVPEIQDYIESLQ
RPRTGSIDGGSSQAIYASSSNSRRGSAMAPGLGLGRKTQLPEAAGVPRQAEWNPRERLER
LRRHQLTFLVNNAYGSRPAPAGYDGRGRHQDRSTGERSQGQEASTTPRPGPRR

Enzyme Prediction     

EC	2.4.1.186:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT8	456	654	1.5e-35	0.8171206225680934

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
133018	GT8_Glycogenin	9.91e-76	456	680	16	240	Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen. Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.
279798	Glyco_transf_8	1.16e-17	456	653	14	248	Glycosyl transferase family 8. This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.
395444	Abhydrolase_1	7.77e-16	95	249	1	147	alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.
132996	Glyco_transf_8	1.58e-14	522	653	84	244	Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.
133037	GT8_A4GalT_like	3.87e-14	456	654	15	247	A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD88986.1|GT8|GT90	1.34e-206	52	1192	591	1647
AJD23148.1|GT8	2.75e-167	25	621	23	781
BCS23823.1|GT8	2.05e-121	456	1192	22	671
CAK43246.1|GT8	2.11e-117	456	1211	21	748
QSS70521.1|GT8	2.95e-116	457	1147	1	607

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1LL2_A	1.46e-43	456	728	19	307	Crystal Structure of Rabbit Muscle Glycogenin Complexed with UDP-glucose and Manganese [Oryctolagus cuniculus],1LL3_A Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus]
4UEG_A	1.52e-43	456	683	19	260	Crystal structure of human glycogenin-2 catalytic domain [Homo sapiens],4UEG_B Crystal structure of human glycogenin-2 catalytic domain [Homo sapiens]
1LL0_A	1.70e-43	456	728	25	313	Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus],1LL0_B Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus],1LL0_C Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus],1LL0_D Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus],1LL0_E Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus],1LL0_F Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus],1LL0_G Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus],1LL0_H Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus],1LL0_I Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus],1LL0_J Crystal Structure of Rabbit Muscle Glycogenin [Oryctolagus cuniculus]
1ZCV_A	1.10e-42	456	728	39	327	Chain A, Glycogenin-1 [Oryctolagus cuniculus]
3V90_A	1.41e-42	456	677	39	273	Structure of T82M glycogenin mutant truncated at residue 270 [Oryctolagus cuniculus],3V91_A Structure of T82M glycogenin mutant truncated at residue 270 complexed with UDP-glucose [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P13280|GLYG_RABIT	7.52e-43	456	728	19	307	Glycogenin-1 OS=Oryctolagus cuniculus OX=9986 GN=GYG1 PE=1 SV=3
sp|H2KYQ5|GYG1_CAEEL	9.41e-42	456	701	18	261	Glycogenin-1 OS=Caenorhabditis elegans OX=6239 GN=gyg-1 PE=1 SV=1
sp|O15488|GLYG2_HUMAN	1.54e-41	456	683	52	293	Glycogenin-2 OS=Homo sapiens OX=9606 GN=GYG2 PE=1 SV=2
sp|Q9R062|GLYG_MOUSE	5.41e-41	456	683	19	259	Glycogenin-1 OS=Mus musculus OX=10090 GN=Gyg1 PE=1 SV=3
sp|O08730|GLYG_RAT	2.10e-39	456	683	19	259	Glycogenin-1 OS=Rattus norvegicus OX=10116 GN=Gyg1 PE=2 SV=4

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000040	0.000002

TMHMM  Annotations     

Start	End
10	32
230	252