CAZyme Information: P174DRAFT_361852-t37_1-p1

Basic Information

• Species: Aspergillus novofumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus novofumigatus
• CAZyme ID: P174DRAFT_361852-t37_1-p1
• CAZy Family: AA3
• CAZyme Description: Anp1-domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
816	MSZS01000001|CGC21	90221.98	6.0950

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnovofumigatusIBT16806	11729	1392255	197	11532

• Gene Location: location=MSZS01000001:4374795-4378481(-)

Full Sequence      

MSKPLQGTAIITGGNGTLGSEIAIAIAKTQPFVHLLLLARDIRTDSVKDLLQKIRLVGPR
SVEVAKVNLASFNSVVSFCQNTVERVRTKEIPPIMLLVNSAAMASYVSDPVTPDGYDPVY
QVNCIAPFLLTVSLLEAFRAGNGTPDGGARVINIGCSAISNGSLNYFDDSPDNAPKPPGT
PLSAKEGNARFGSSKLIMSAAMYALRRSLVLTGNMSLNIYTLDPGGLEGNSHLTTDAPLS
VRMAHSTRSSLGPFLRVFSKSAINKASVPAKVVAKVAFQRETVELWGRERYYILDSDYEA
GSVILALRDPPLMDSLLKKIFQPRPQSALRRRRLLIQRLCLIGGISLLILVLIFPSWRAA
ILPTLSLGLIHSSEDIQLQTVRYYDLSKVQGTAQGWEKGERVLMLTPLRDASSHLPMFFS
HLRNLTYPHNLIDLAFLVSDSKDDTLGMLTRMLEEVQNDTDPKMTFGEISVIQKDFGQKV
QQDVESRHGFAAQAGRRKLMAQARNWLLSATLRPTHSWVYWRDADVETAPRTILEDLMRH
DKDVIVPNVWRPLPDWLGGEQPYDLNSWQESETALALAETLDEDAVIVEGYAEYATWRPH
LAYLRDPFGDPDMEMELDGVGGVSILAKAKVFRSGVHFPAFSFEKHAETEAFGKMAKRMG
FSVIGLPHYTIWHLYEPSVDDLRHMEEMEQERKAREREEKEQAERAERMKALFVEPGPQW
DIDKAFVEDSIQIEKQEAGQTKADGVTGAAEVKDVQDSIQIEKQEAGQTKADGVTGAAEV
KDVQDSASHPVAASPKPSVNAAPVVRGRPGEAERSI

Enzyme Prediction     

No EC number prediction in P174DRAFT_361852-t37_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT62	379	642	6.1e-125	0.9888059701492538

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397491	Anp1	6.72e-160	380	642	1	265	Anp1. The members of this family (Anp1, Van1 and Mnn9) are membrane proteins required for proper Golgi function. These proteins co-localize within the cis Golgi, and that they are physically associated in two distinct complexes.
212492	retinol-DH_like_SDR_c_like	8.06e-24	8	225	3	195	retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs. Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
212491	SDR_c	2.43e-11	9	155	1	132	classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
187670	LPOR_like_SDR_c_like	2.18e-09	6	200	1	176	light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs. Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
395056	adh_short	2.48e-09	8	155	2	135	short chain dehydrogenase. This family contains a wide variety of dehydrogenases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAA64203.1|GT62	0.0	1	754	1	757
QRD89585.1|GT62	3.49e-238	321	755	29	463
BAE60428.1|GT62	4.83e-238	321	737	4	420
QMW42749.1|GT62	9.94e-238	321	755	58	492
QMW30696.1|GT62	9.94e-238	321	755	58	492

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZF8_A	4.81e-59	381	678	6	304	Crystal structure of Saccharomyces cerevisiae Mnn9 in complex with GDP and Mn. [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P32629|ANP1_YEAST	2.53e-154	380	685	61	366	Mannan polymerase II complex ANP1 subunit OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ANP1 PE=1 SV=3
sp|O74745|ANP1_SCHPO	1.82e-145	381	687	77	385	Mannan polymerase II complex anp1 subunit OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=anp1 PE=3 SV=1
sp|P23642|VAN1_YEAST	2.20e-118	380	685	171	523	Mannan polymerase I complex VAN1 subunit OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=VAN1 PE=1 SV=3
sp|Q00314|VAN1_CANAX	1.01e-117	372	685	67	430	Vanadate resistance protein OS=Candida albicans OX=5476 GN=VAN1 PE=3 SV=1
sp|P53697|MNN9_CANAL	9.32e-65	374	676	66	368	Mannan polymerase complex subunit MNN9 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MNN9 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000087	0.000000

TMHMM  Annotations     

Start	End
339	361