CAZyme Information: GAQ05094.1

Basic Information

• Species: Aspergillus lentulus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus
• CAZyme ID: GAQ05094.1
• CAZy Family: GH1
• CAZyme Description: PNP_UDP_1 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0S7DMG9]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2458	BCLY01000004|CGC33	272148.40	6.1423

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlentulusIFM54703	9916	N/A	259	9657

• Gene Location: location=BCLY01000004:3532541-3543778(-)

Full Sequence      

MAAPPPSYTKVTHSATYASINPTKAGLSTAGKVVLITGASGGIGRAAASSFAASRPRALI
LLGRRADALAETATIVRASHAEVAIQTHTAELCDASGVRNAMDKVAAEFGGIDILVHCAG
VLAPVVPLLEADPATFLDGYKTTVVGTLVTAQAVVLANKTVSTNEDKPVTFINLTTAGIL
FPPFPGMGAYVSSKMAAVKLLEAFAAENPQVRLHNVHPGLLKTAMSAKLAEKIKLPYAYD
DISLPADFLVWIASPEAEFLKNKIVFAAWDVDELKGRKKEIVGGPPGTGDNNTGKALSND
DYIVGWICATTTEYVAAQAFLDESHGRPNYVCVNDNNDYRLGEIGEHNVVIAVLPGYGIA
PAACVARDMLHSFPNVRICLMVGIGGGAPSSKHDIRLGDIVVSTPNEGTGGVFQYDFGKT
IQDQSFQHTGFLNQPPIFLQTAVNGLKAQYMSGGHHLNEAINNILEKKPRLQPIYKRPDS
VTDRLYESNVVHPPQCQRSCAVVCGNDPTKLIKRRERGEHEDSPAIHYGTIASANQLMKD
ASIRDKLAAEKGVLCFEMEAAGLTNHFPCLIIRGICDYSDSHKNDDWQGYAAMAAAAYAK
DLLSRIPPTTAERQKRIAEQFSGNLATTAGEMADPQKNKNPQEYACDYSHAHKSKEWQRY
AAATAAAYARELLEELPVAEASARVTSMPNPPNEENQDAFKIERGNFDVELVPFFTERSI
EINQIRQLFQPSRSRTTVVLHGLGGIGKTQIALKYANDYKEEYSAIFWVNHRSTDTVKQS
LFAAAERVHRKYPSWPGLKEALESNDTNKACLTVIDWLSQDQNNQWLVICDGYDQCQTDD
SKQGNWDLHRMLQAHHGHILITSRWRQSDLWHHVQIEKFTDLSHGVDLLLKRSSRSSLRD
DPDIQTLAETLDGLPLALVAAGAYLGISLFSCSKYLLVYNKSWLRLLKETPTSDAYDRTL
YSTWNLTWERICTVNELAANLLRFCAYFDNKGLWFELFQMGNELDKPEWLQRLTEDEFEF
DVAVRILREHALVEEQAGGRHGESGSIRFSIHNCVHSWTIHVLNENWNYGMSSVALGCIA
SKIPQKSTPSFWHISQRLLAHANRIVDLFSQKRLIQVYTETQLEQMRDVIEAQVEQMQGV
IYFFLERDRPETVEKMCISLHEQVEKMFGYYHPATFTLKWLMISIFTSLKNYDEAETLCN
RTLSRFNNNPDVNEGRAKRSFTLLLAQICMLRGQTEKGEELLLGPSTSPQDAGISGLLFE
ENLVSRLWTQYLAQDMSRDMQTWMENHLLKEETGKAGSCQQSFNLLCTQIYLCLSQNKNE
EAKALLLEAREMFDRENSADYAKASIFSDLAALYIKLGEYGDLMCLCDDATTGDWESLWQ
SDVRFSCTVVLMRCYVHLNRDELDETVDLCQRALKKLHNSRVLAAAPKRSVLIMLGSVYM
QQGKLLEAEKHFAAAIQETRESKQQSFYVVQSGAVALYTLLAAVAVSASGVDSGFVNPDV
VYRPKFRYWLPDASVPADVVQEDIARIAEAGGGGIELLPFYLYGLPTAQGMNATPPSDWN
VYGFGTPAFNDLFQAALNGSKESKVRMDFAVGANQGQGVPAVPGTPGLAVQLLLGSTSVH
AGQRYSSTVPPPAELSSVLQSGLTFMHPLEDFSTPNLTAVIAYQVLNDSSSGGSKIVALD
PLSFIDLSAKVKDGLLDWTAPLGNSTWRVFSFWVKHTNQRSCTGGRDATTVIGNGSWTVD
HFDAMGARLITDFWDQYILSDEQTLTFLQEVGQYGTVSSFVLHKNATDDFVAWEDSMEML
SSLYWTPSLLSRFEQDRGYSALSCLPALFKPQNNWNAIVPSYNEMYTLGDQKDSACNADY
RRTLNAGYQDYIAHFSQWANRIGIQYSNQPAYNLPLEMLGDIPLSDAPECESLGFSDNID
AYRQFSGPAHISNRNVISNEMGAVNKPAYMLTIPELLYSIKRAWSGGVNMVVLHGYTYSG
NYPNTTWPGYTTFGYGFTEMWNQIQPAWIHMKDYLDYISRNQFVLQQGRPQIDLALYLYE
TPWSAVDLLRSNNITAAGYTHDYVAPDSLVPPQVTVRAKVLAPDGPSYKALIFASPKFNI
STFNLVREDVAARVVEFARKGLPVIFVGGLPQVTSNTQAGQIVEDGWRKIRNLPSVQFIS
SLADLPGALSKAGVTPNVLPSCTTGTLRVVKRSRPEDEVDYVFLYNDQIVSTSCQISIQD
HGARTPHLLNAWTGEKKMIGSFERRSALITVSLQFAPNETSILSLEKSGSSDPTDLIMLA
SSSASSRYGIANLTRWDLSIEDFHAPRRRSQVQTAITSHNFSNIALRPWSAISPALINVG
GIGRYSTSFTVPNVPRIQGKLSLGPIIHTARVYIGGRRLPPIDPVNPVIDISSYISPSQT
YKIIVEVTTPLFNRIKTDANQTKIAGSTAGELQPLYASTPYQEYGLMGPVVLTWSISS

Enzyme Prediction     

No EC number prediction in GAQ05094.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH106	1492	2453	3.9e-82	0.9951456310679612

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
212491	SDR_c	1.74e-30	34	260	1	226	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.
223959	FabG	1.43e-26	27	284	1	249	NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only].
407266	Glyco_hydro_106	5.97e-25	1678	2240	347	870	alpha-L-rhamnosidase.
235975	FabG-like	9.83e-25	30	260	4	237	SDR family oxidoreductase.
395056	adh_short	1.11e-24	32	233	1	194	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
UPK96040.1|GH0	4.42e-194	1470	2452	45	1031
CZS85684.1|GH106	5.58e-186	1494	2452	60	1022
CEF85836.1|GH106	7.68e-186	1494	2452	60	1022
UQC81996.1|GH106	8.95e-185	1473	2454	5	1042
QKD46519.1|GH106	2.74e-184	1489	2450	27	1011

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3G1T_A	5.64e-13	32	236	15	220	Chain A, short chain dehydrogenase [Salmonella enterica subsp. enterica serovar Typhi]
3IAH_A	8.69e-11	32	236	16	221	Crystal Structure of Short Chain Dehydrogenase (yciK) from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 in Complex with NADP and Acetate. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3IAH_B Crystal Structure of Short Chain Dehydrogenase (yciK) from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 in Complex with NADP and Acetate. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
3F5Q_A	3.09e-10	32	236	15	219	CRYSTAL STRUCTURE OF putative short chain dehydrogenase from Escherichia coli CFT073 [Escherichia coli O6],3F5Q_B CRYSTAL STRUCTURE OF putative short chain dehydrogenase from Escherichia coli CFT073 [Escherichia coli O6],3GZ4_A Crystal structure of putative short chain dehydrogenase FROM ESCHERICHIA COLI CFT073 complexed with NADPH [Escherichia coli O6],3GZ4_B Crystal structure of putative short chain dehydrogenase FROM ESCHERICHIA COLI CFT073 complexed with NADPH [Escherichia coli O6]
3I1J_A	3.38e-10	31	228	14	208	Structure of a putative short chain dehydrogenase from Pseudomonas syringae [Pseudomonas syringae pv. tomato],3I1J_B Structure of a putative short chain dehydrogenase from Pseudomonas syringae [Pseudomonas syringae pv. tomato]
3F1L_A	8.83e-10	32	236	13	217	The 0.95 A structure of an oxidoreductase, yciK from E.coli [Escherichia coli K-12],3F1L_B The 0.95 A structure of an oxidoreductase, yciK from E.coli [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|M1W848|PIG17_CLAP2	3.74e-24	6	282	15	280	Short chain dehydrogenase/reductase CPUR_05418 OS=Claviceps purpurea (strain 20.1) OX=1111077 GN=CPUR_05418 PE=1 SV=1
sp|A0A144Y7G4|CITE_MONPU	6.85e-24	1	284	1	283	Short chain dehydrogenase mpl6 OS=Monascus purpureus OX=5098 GN=mpl6 PE=1 SV=1
sp|A0A162J3X8|CITE_MONRU	6.85e-24	1	284	1	283	Short chain dehydrogenase citE OS=Monascus ruber OX=89489 GN=citE PE=1 SV=1
sp|A0A2I1C3V7|NSRO_ASPN1	8.89e-24	6	282	8	278	Short chain dehydrogenase/reductase nsrO OS=Aspergillus novofumigatus (strain IBT 16806) OX=1392255 GN=nsrO PE=1 SV=1
sp|A0A1L9WLF6|AACUD_ASPA1	1.62e-22	9	274	11	264	Short chain dehydrogenase/reductase AacuD OS=Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094) OX=690307 GN=AacuD PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000056	0.000000

TMHMM  Annotations     

There is no transmembrane helices in GAQ05094.1.