CAZyme Information: XP_001906534.1

Basic Information

• Species: Podospora anserina
• Lineage: Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina
• CAZyme ID: XP_001906534.1
• CAZy Family: GH12
• CAZyme Description: Podospora anserina S mat+ genomic DNA chromosome 1, supercontig 6 [Source:UniProtKB/TrEMBL;Acc:B2AS32]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
726	CU633897|CGC1	78264.75	9.0042

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PanserinaSmat	10888	515849	370	10518

• Gene Location: location=CU633897:277993-280351(-)

Full Sequence      

MEAGCFKRDHDPPLSVLWRERYEIGTKSPPPQTLIMKFSPATLLPLLMAAGSNAAPSQNS
PRQTKPPTVYLAGDSTMARTNSPHNGWGEYLSRYLTISVVNKAISGRSARSFTNEGRFAE
IERLVVPNDIVIISFGHNDGSSPNSANDNGRSACPGTGNEVCRSGKTGETVYTYNHYLQT
AGRALIAKGAKVVFSAQTPKNLWQNGQWSGNYEPPRFVPYAAAAARNVGSGASFVDHYQA
VTKTYQRLGSQKVNSFYPVDYTHTSPEGADVIAQAFAQAVSRDFNGTTAVKPYLRNPVPN
PSAAIGICMTRVGVVVARGVCDAGRCCLRVAGSDIGHLFFFQSPIQFSVPGIHQFSSPAK
AVQRTMAKVLITGINGYIAAHTAARFLQAGFSVRGTVRNKTSPNVESLLRALSAPQKAGG
GKVEIVEVPDITIEGAFDNAVQAHLASPVSMADGDPAPMMKAAVDGTTSLLASAVEAPTK
FKSVAFMSSISAVYSPPPYRSPDHVFTSADWNQEAEAKVAELGDNTPGYITYQASKTAAE
KALWKIVDDKNDPRWKAVNVTTFCPSPVLGPPLFMPSPLSGLSMRVKDIWDVMHGGDVPE
ASVIRGTFVDVRDVAEVVVKTVANDLAVGDGEEKRRERLLLVAQDNVSPGQMAQVLREEV
GDNLRGVIREASAGKVEEVKKTRAAMKKFNSEPARKVLGRDWVMFRDSVVDSARFFVSFE
ETEAII

Enzyme Prediction     

No EC number prediction in XP_001906534.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE12	68	279	9.5e-45	0.9904761904761905

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
187538	AR_SDR_e	1.01e-55	368	699	1	301	aldehyde reductase, extended (e) SDRs. This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.
238859	Rhamnogalacturan_acetylesterase_like	2.50e-53	67	280	1	198	Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
187661	FR_SDR_e	2.81e-30	369	616	1	227	flavonoid reductase (FR), extended (e) SDRs. This subgroup contains FRs of the extended SDR-type and related proteins. These FRs act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites; they have the characteristic active site triad of the SDRs (though not the upstream active site Asn) and a NADP-binding motif that is very similar to the typical extended SDR motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.
187536	AR_like_SDR_e	8.90e-27	369	658	1	266	aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs. This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.
223528	WcaG	4.61e-24	368	699	2	290	Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAP67203.1|CE12	0.0	1	726	1	726
CDP24616.1|CE12	0.0	1	726	1	726
AEO61153.1|CE12	2.06e-109	47	299	12	260
AEO64902.1|CE12	4.32e-105	43	299	8	260
QPC78219.1|CE12	1.68e-86	68	300	22	255

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1DEO_A	3.27e-64	68	280	2	212	RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.55 A RESOLUTION WITH SO4 IN THE ACTIVE SITE [Aspergillus aculeatus],1DEX_A RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.9 A RESOLUTION [Aspergillus aculeatus],1K7C_A Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution [Aspergillus aculeatus],1PP4_A The crystal structure of rhamnogalacturonan acetylesterase in space group P3121 [Aspergillus aculeatus],1PP4_B The crystal structure of rhamnogalacturonan acetylesterase in space group P3121 [Aspergillus aculeatus]
3C1U_A	1.72e-63	68	280	2	212	Chain A, Rhamnogalacturonan acetylesterase [Aspergillus aculeatus]
5GMO_A	1.87e-19	369	714	5	327	Chain A, Protein induced by osmotic stress [Scheffersomyces stipitis CBS 6054],5YW4_A Chain A, Protein induced by osmotic stress [Scheffersomyces stipitis CBS 6054]
5YWL_A	1.87e-19	369	714	5	327	Chain A, Protein induced by osmotic stress [Scheffersomyces stipitis CBS 6054],5YWN_A Chain A, Protein induced by osmotic stress [Scheffersomyces stipitis CBS 6054]
1Y1P_A	4.65e-15	369	581	14	220	X-ray structure of aldehyde reductase with NADPH [Sporidiobolus salmonicolor],1Y1P_B X-ray structure of aldehyde reductase with NADPH [Sporidiobolus salmonicolor],1ZZE_A X-ray Structure of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor [Sporidiobolus salmonicolor],1ZZE_B X-ray Structure of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor [Sporidiobolus salmonicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q00017|RHA1_ASPAC	2.88e-63	68	280	19	229	Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 SV=1
sp|Q5BAA2|RHA1_EMENI	9.62e-56	68	280	19	224	Rhamnogalacturonan acetylesterase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN2528 PE=1 SV=1
sp|Q9UT59|YKJ7_SCHPO	3.16e-22	369	659	6	279	Putative uncharacterized oxidoreductase C513.07 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC513.07 PE=3 SV=1
sp|O94563|YGD4_SCHPO	8.44e-21	369	620	5	250	Putative uncharacterized oxidoreductase C1773.04 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPBC1773.04 PE=1 SV=1
sp|O31528|RHGT2_BACSU	9.48e-17	69	280	5	202	Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.975628	0.024377

TMHMM  Annotations     

There is no transmembrane helices in XP_001906534.1.