CAZyme Information: jhhlp_001710-t41_1-p1

Basic Information

• Species: Lomentospora prolificans
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
• CAZyme ID: jhhlp_001710-t41_1-p1
• CAZy Family: AA7
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1226	NLAX01000005|CGC2	134665.55	5.0136

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LprolificansJHH5317	8768	N/A	208	8560

• Gene Location: location=NLAX01000005:169878-174699(+)

Full Sequence      

MTKLKTSSIPLLFLAGSSVASPAPLAQDSVFFRVPESVSSESVHNVHITYGDKLPQGNVN
IVYGDCASRDVGQSHHEVATLFLSGSDSMPDRLVWSVPKDVTQRGCLHAFSESRLLGRSE
PVSFSESLQKRESLHEIGDSTGLWFNGVKYLKSTDKSTTVTDAAKSKKIAIIGGGISGLM
TSLLLTSVGINDWHIIESTERIGGRIRTKYLNGTSPSDYQYQEMGPMRFPVSIRYSDTNE
TLDIQDHKMVFQLADVLNEMNGNSSDLAVNFIPWIQSNPNTPANSRGGRLPNGQIPSSAQ
IAADPSLRNPSATAADPEEAELASEFVEHFLDFTPERMRNISTNIFQAHREAIDKGLFHW
SETAFLRYKLGLDADTVDLLSGSDNSPMWEEWYDNTYFGATTWRTIDKGLNSLPRAFEPH
VQGKITYGRKVEGLAYDNATSKVSVNWRDDEFAMVPQSEEYDYAMVAVPFSKVRLWRTPQ
YSSLLSRAISTLNYAQSCKVALHYKTRFWEHQENPIFGGCGSADIPGVSSICYPSYQINS
TGPGVILGSYVSGTMARSVAALSEKDHVAMIQRAMVEVHGEIANEEYTGNYNRQCWEVDE
HQAGAWASPTVGQQELFIPAYHNTEYNTIFIGEHTSITHAWIFSALESAVRGTTQLLLDL
GLVDEAKQVKPHSVRFSEDGFGDGPVQVSLPSWQWPGTYTYIDAFQDAGIQIRTDGGSNG
VNVGFNWNPSDIDPVNGTRSSSRKAYWDPASERPNLSIIVNTFVSTVSFENKTASGVNII
SRDTGDTVFVPASAEVILAAGSVHTPQILQLSGIGPRDLLQELDIEEVVDLPGVGSNFQD
HLSISTAWRFTSEPEVNPSILRDPDFLDAAFDEYWANKSGPITHTGKSCRVMLSLHNLTD
EVDSIVSTLEEEDPAQYLGDVYLASEELLAGYKAQHAILSRMVGSDEVSVFEHTFGGGAD
MSFHPQKPFSRGTIRIKSTDPHPADSPPQVDFRAMTHPLDMQIAILGLKFGRNILNGDIM
GELGSREVSPGANVTSDDELEQFLRTRAVGGLLGAEVFAALQKEGVFTVSVLSLSSSKST
FPSHIQVYKLDDDYPLDQLVGAFKGKNALVSTLPGRPYAGHIRMVDVAVQAGVKRFIPSE
YGNNTCAGAAEQVDLYADKAKIITHLKSKENTGLTWTAIHTGQFFDWGMESGWLNYCLDG
RRVTIYNSGNKPWSTSTLGRQSPIKA

Enzyme Prediction     

No EC number prediction in jhhlp_001710-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA3	671	1048	2.3e-83	0.6390845070422535

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
235000	PRK02106	1.30e-47	678	1048	138	468	choline dehydrogenase; Validated
225186	BetA	7.19e-42	682	1048	147	469	Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only].
396255	Amino_oxidase	7.54e-35	179	651	4	440	Flavin containing amine oxidoreductase. This family consists of various amine oxidases, including maze polyamine oxidase (PAO) and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
187569	PCBER_SDR_a	3.11e-31	1050	1218	8	178	phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs. PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.
224152	YobN	2.63e-27	409	657	207	444	Monoamine oxidase [Amino acid transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UQC77231.1|AA3_2	1.25e-83	669	1062	175	569
UPK99906.1|AA3_2	3.35e-73	669	1045	172	546
QSS75262.1|AA3_2	2.54e-69	669	1053	45	423
SMR50915.1|AA3_2	3.25e-65	684	1043	191	548
SMR51855.1|AA3_2	3.25e-65	684	1043	191	548

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZE2_A	7.99e-45	684	1045	153	514	Chain A, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],6ZE2_B Chain B, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],6ZE3_A Chain A, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],6ZE4_A Chain A, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],6ZE4_B Chain B, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],6ZE5_A Chain A, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],6ZE5_B Chain B, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],6ZE6_A Chain A, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],6ZE6_B Chain B, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],6ZE7_A Chain A, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],6ZE7_B Chain B, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],7AA2_A Chain A, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495],7AA2_B Chain B, FAD-dependent oxidoreductase [Thermochaetoides thermophila DSM 1495]
6O9N_A	4.55e-36	680	1048	191	573	Structural insights on a new fungal aryl-alcohol oxidase [Thermothelomyces thermophilus],6O9N_B Structural insights on a new fungal aryl-alcohol oxidase [Thermothelomyces thermophilus]
7C3I_A	5.21e-24	167	657	8	492	Structure of L-lysine oxidase D212A/D315A [Trichoderma viride],7C3I_B Structure of L-lysine oxidase D212A/D315A [Trichoderma viride],7C3J_A Structure of L-lysine oxidase D212A/D315A in complex with L-phenylalanine [Trichoderma viride],7C3J_B Structure of L-lysine oxidase D212A/D315A in complex with L-phenylalanine [Trichoderma viride],7C3L_A Structure of L-lysine oxidase D212A/D315A in complex with L-tyrosine [Trichoderma viride],7C3L_B Structure of L-lysine oxidase D212A/D315A in complex with L-tyrosine [Trichoderma viride]
7C3H_A	3.83e-23	167	657	8	492	Structure of L-lysine oxidase in complex with L-lysine [Trichoderma viride],7C3H_B Structure of L-lysine oxidase in complex with L-lysine [Trichoderma viride]
3X0V_A	3.85e-23	167	657	8	492	Structure of L-lysine oxidase [Trichoderma viride],3X0V_B Structure of L-lysine oxidase [Trichoderma viride]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23623|OXLA_NEUCR	3.09e-162	15	667	16	683	L-amino-acid oxidase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=lox PE=1 SV=2
sp|Q5AUN2|XPTC_EMENI	3.20e-45	683	1045	184	545	Dehydrogenase xptC OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=xptC PE=3 SV=1
sp|Q0CJ60|ATC_ASPTN	4.58e-33	684	1051	193	531	Cyclase atC OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=atC PE=1 SV=1
sp|A7MFA8|BETA_CROS8	1.32e-32	682	1065	141	492	Oxygen-dependent choline dehydrogenase OS=Cronobacter sakazakii (strain ATCC BAA-894) OX=290339 GN=betA PE=3 SV=1
sp|A5WA97|BETA_PSEP1	1.41e-32	682	1048	143	470	Oxygen-dependent choline dehydrogenase OS=Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1) OX=351746 GN=betA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000438	0.999556	CS pos: 20-21. Pr: 0.9852

TMHMM  Annotations     

There is no transmembrane helices in jhhlp_001710-t41_1-p1.