CAZyme Information: TSTA_023640-t26_1-p1

Basic Information

• Species: Talaromyces stipitatus
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces stipitatus
• CAZyme ID: TSTA_023640-t26_1-p1
• CAZy Family: AA7
• CAZyme Description: FAD binding domain protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
500		54511.74	4.4043

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TstipitatusATCC10500	12629	441959	146	12483

• Gene Location: location=EQ962654:86379-88133(+)

Full Sequence      

MFDILGVVRLTAEMKVFGIGVILALPLLATAQSYNLTALFQPVLSPGAEIYYANDSDWTQ
NVTQRWTTWDAPTYLGAIKPVTERDVQNIVKVASAHNISFLATGGGHGVSQGFANIQNAI
EIDLANFKTVNLDIENNQLTVGGGATYGQLYDPLYNAGKEFPTGNAPCVGVIGATIGAGV
GLLQGLHGYTSDALISARIVTASGVLFEASATNNTELFWAIRGAGANFGIITSATYRIYD
ATNSGQAQNADFLFAESANRTVWNALQTLDETLPAELSVTITSTYNQTSGQASIMVNLVY
FGIYDNFQPYVDQFLAISPTQWRNVTVPWNQLIASANFGAPSHGCGTNSSHINFFSIALN
QTDPLTFQGFFDDLILFSQQNPSYTGAWVIERYSTQGPLAVPEETRGVYPWREAKMQLLW
ESDYPDSSLDSTVNAFYTQQRQHFDEFSGFHTFATYVNYAHGDEGPNVWYGDADNLARLS
AAKRKWDSNNLFGAAKPVPL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	80	288	3.8e-51	0.4497816593886463

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.24e-25	69	258	23	223	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	6.50e-25	75	210	2	139	FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
273751	FAD_lactone_ox	4.32e-09	65	270	3	201	sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
178402	PLN02805	9.74e-07	80	238	140	304	D-lactate dehydrogenase [cytochrome]
369658	BBE	1.39e-06	455	499	1	45	Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK90596.1|AA7	7.48e-28	73	498	19	441
QRC92907.1|AA7	1.02e-26	80	339	69	327
CCA69005.1|AA7	6.25e-22	78	500	62	486
QRW22693.1|AA7	2.72e-21	78	500	65	484
VBB87167.1|AA7	9.76e-20	42	241	40	233

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO4_A	1.20e-32	37	500	12	470	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	2.24e-32	37	500	12	470	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6Y0R_AAA	1.56e-24	80	492	67	482	Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
5K8E_A	5.59e-23	79	291	66	283	Xylooligosaccharide oxidase from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],5L6F_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylobiose [Thermothelomyces thermophilus ATCC 42464],5L6G_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylose [Thermothelomyces thermophilus ATCC 42464]
2BVF_A	4.84e-21	44	240	10	204	Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVF_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVG_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVH_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G3XMD0|AZAL_ASPNA	5.35e-151	23	483	10	471	FAD-linked oxidoreductase azaL OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaL PE=2 SV=2
sp|G3XMC1|AZAG_ASPNA	2.94e-136	29	479	16	468	FAD-linked oxidoreductase azaG OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaG PE=2 SV=1
sp|Q4WLW6|FMQD_ASPFU	1.47e-124	35	500	33	495	FAD-linked oxidoreductase fmqD OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fmqD PE=1 SV=1
sp|Q0CF74|AZPB3_ASPTN	3.26e-119	31	498	22	480	FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1
sp|Q5BEJ5|AFOF_EMENI	1.65e-116	29	499	14	479	FAD-linked oxidoreductase afoF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afoF PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.300001	0.699980	CS pos: 31-32. Pr: 0.6801

TMHMM  Annotations     

There is no transmembrane helices in TSTA_023640-t26_1-p1.