CAZyme Information: FOC1_g10000349-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOC1_g10000349-t38_1-p1
• CAZy Family: AA1
• CAZyme Description: Pectate lyase A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
336		36972.73	7.3571

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporumrace1	15626	1229664	188	15438

• Gene Location: location=KB731247:15217-16380(+)

Full Sequence      

MKLSSVLCGVFATLTVAFPKEYLSLATWGVEGYAKDNPIGITTGGKGGKIVTVTTAEELV
AAVKGTEPKIVKLKGKVTLPSRLKVGSNTSLIGVGLTAHITGAGVDVYHGDNVILQNLKI
THILDNDCITIRNSTRVWVDHNEFSSDINQGPDHYDGQVDIIRASDWITVSWNYFHDHWK
SSLVGNDATFRDLDFGHLHITYHHNYWRNMGTRGPAGRFGHQHVYNNLYEDFLYQAIHSR
SDNQVLVEGNVFRGNTSEALSTYGLVIPMDSPNTCTCGDEELDGYANLGAKNDWGKAGVN
ITQKGNFYKADYKYKLTPLKLVPTVAKLGAGVGRIW

Enzyme Prediction     

No EC number prediction in FOC1_g10000349-t38_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL1	80	253	3.2e-107	0.9943181818181818

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214765	Amb_all	1.45e-56	83	252	12	186	Amb_all domain.
226384	PelB	5.62e-54	51	335	57	344	Pectate lyase [Carbohydrate transport and metabolism].
366158	Pec_lyase_C	1.12e-34	81	252	28	211	Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD49282.1|PL1_10	2.50e-256	1	336	1	336
QGI68220.1|PL1_10	3.01e-252	1	336	1	336
QGI99110.1|CBM50|PL1_10	3.06e-248	1	336	1	339
CCT73126.1|PL1_10	2.21e-238	21	336	6	324
CAW61457.1|PL1_10	5.88e-230	1	336	1	336

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VMV_A	2.11e-40	29	335	3	325	Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5]
1VBL_A	3.45e-32	85	335	130	415	Structure of the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
3ZSC_A	1.87e-30	36	335	16	331	Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
5AMV_A	3.88e-26	85	230	125	296	Structural insights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168]
1PCL_A	4.11e-26	32	252	10	276	Chain A, PECTATE LYASE E [Dickeya chrysanthemi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q5AVN4|PLYA_EMENI	1.80e-55	32	316	44	307	Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1
sp|Q8GCB2|PTLY_BACLI	3.69e-55	9	335	14	339	Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
sp|Q65DC2|PTLY_BACLD	3.69e-55	9	335	14	339	Pectate trisaccharide-lyase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi04129 PE=3 SV=1
sp|B1B6T1|PTLY_BACSP	3.69e-55	9	335	14	339	Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
sp|Q2TZY0|PLYB_ASPOR	3.82e-54	1	260	1	266	Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000251	0.999738	CS pos: 17-18. Pr: 0.9814

TMHMM  Annotations     

There is no transmembrane helices in FOC1_g10000349-t38_1-p1.