CAZyme Information: PMAA_015700-t26_1-p1

Basic Information

• Species: Talaromyces marneffei
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces marneffei
• CAZyme ID: PMAA_015700-t26_1-p1
• CAZy Family: AA7
• CAZyme Description: FAD binding domain protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
486	DS995899|CGC10	52872.77	4.4327

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmarneffeiATCC18224	10194	441960	145	10049

• Gene Location: location=DS995899:115792-117511(+)

Full Sequence      

MTRFSIPSILALPLLAAAQSYNLTALFAPVLSPTAEIYYANDSNWTQEVTQRWSTWDAPT
YLGAIKPVTERDVQNIVKVASARNISFLATGGGHGVSQGFAKVQNAIDIDLSNFKTVDLD
VENNRVTVGGGATYGQLYDPLYNAGKEIPTGNAPCVGVVGATVGAGVGLLQGLHGYTSDA
LISARIVTASGVLFEASATNNTELFWAIRGAGANFGIITSATYKVYDATNAGQAQNADFL
YPEISNRTVWGTLQTLDETLPAELSVTITSAYNQTSGQAAIIVNLVYFGAYDDFRPYVDQ
FVAINPTQWRNVTAPWNELVEAANFGAPSHGCGTDSHINFFSIALNQTDPLTFQGFFDDL
ILFSQQNPSYNGAWVIERYGTQGPLAIPEESRGVYPWREAKIQLLWESSYPDSSLDDTVR
AFYTQQRQHFNEFSGFPTFAAYVNYAHGDEGPNVWYGDADNLSRLSAAKRKWDSNNLFGA
AKPVPL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	67	274	6.7e-53	0.44759825327510916

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	7.18e-25	62	197	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.
223354	GlcD	1.16e-24	56	239	23	217	FAD/FMN-containing dehydrogenase [Energy production and conversion].
273751	FAD_lactone_ox	1.78e-09	52	225	3	178	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.
369658	BBE	6.10e-07	441	485	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.
223882	MurB	2.43e-05	65	236	25	187	UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	1.40e-27	67	345	69	346
CCA69005.1|AA7	9.28e-27	65	486	62	486
UPK90596.1|AA7	1.39e-26	60	484	19	441
QRW22693.1|AA7	4.69e-24	65	486	65	484
QGA17347.1|AA7	3.03e-21	67	486	54	473

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO4_A	2.09e-33	67	486	54	470	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	3.90e-33	67	486	54	470	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6Y0R_AAA	3.78e-26	67	478	67	482	Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
5K8E_A	4.98e-23	66	278	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	3.08e-22	28	227	7	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	4.05e-152	10	469	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	9.09e-137	16	465	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	8.33e-123	22	486	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|Q5BEJ5|AFOF_EMENI	1.29e-120	3	485	2	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
sp|Q0CF74|AZPB3_ASPTN	7.28e-120	18	484	22	480	FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000354	0.999609	CS pos: 18-19. Pr: 0.9776

TMHMM  Annotations     

There is no transmembrane helices in PMAA_015700-t26_1-p1.