CAZyme Information: FOZG_10137-t36_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOZG_10137-t36_1-p1
• CAZy Family: GH2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
545	JH717901.1|CGC11	58277.67	4.5795

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumFo47	18556	660027	365	18191

• Gene Location: location=JH717901.1:1699116-1701186(-)

Full Sequence      

MHSSTTLLLLATATVNAIGKRDDCKDVHIFLAKGNNEPYPGRQGKLAGAICSGLKSCDYE
DIQFQNALEDPFCDSVTEGVKNGIKQITAYNKKCPDSKLVVSGYSQGGQVVGDILGGGGG
VFFQNCVEPDLQGLNPKTLPGSKIVAAMVFGDTRHTKDQPFNVLSGAGKNGLFPRPAGML
QNLASYGDVFRNYCVETDPICAQGDEVETHLNYFDVFTDDVAEWVKERIGEDATTTTAAT
KTSTKAKSTAKSTAKETSTKDAETESTTEAASTTKDASKDSTTKDTATAAASTTADSSST
TDASSAEGRATAGEASSGAAAPSSTDNAATSKEWSLPDPPLTEKGEEQCAHLRENLISTF
SDKADNIDDVAIVVSPMRRTMQTAMLSLGWLVERGVKIEGNADWQENSSKPCDTGSPISS
VSPSFPKVNFSSVDPLWPDKTSPSAERYWYTKKSILARGQRALEDLKKRPEKLIFVVSHA
GFLRLGVAGYWFFNSDYRVFDFDGQGIKQQEGTLAGGMGLSLTEPVELGLDLPEEDPGYD
AEVKE

Enzyme Prediction     

No EC number prediction in FOZG_10137-t36_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE5	24	228	2.8e-34	0.9841269841269841

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395860	Cutinase	7.69e-27	24	229	2	173	Cutinase.
395236	His_Phos_1	9.22e-13	337	506	21	185	Histidine phosphatase superfamily (branch 1). The histidine phosphatase superfamily is so named because catalysis centers on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.
223483	PhoE	5.27e-12	337	488	25	162	Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism].
214859	PGAM	6.90e-12	337	484	22	156	Phosphoglycerate mutase family. Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.
132718	HP_PGM_like	3.58e-07	337	386	22	65	Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction. Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGI65106.1|CE5	8.80e-165	1	239	1	239
CCT69066.1|CE5	8.80e-165	1	239	1	239
QGI95990.1|CE5	8.80e-165	1	239	1	239
QGI82360.1|CE5	8.80e-165	1	239	1	239
UPL04270.1|CE5	4.93e-123	1	229	1	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1BS9_A	1.79e-13	24	230	2	207	Acetylxylan Esterase From P. Purpurogenum Refined At 1.10 Angstroms [Talaromyces purpureogenus]
1G66_A	1.79e-13	24	230	2	207	ACETYLXYLAN ESTERASE AT 0.90 ANGSTROM RESOLUTION [Talaromyces purpureogenus]
2AXE_A	1.79e-13	24	230	2	207	Iodinated Complex Of Acetyl Xylan Esterase At 1.80 Angstroms [Talaromyces purpureogenus]
1QOZ_A	4.46e-13	24	213	2	190	Chain A, ACETYL XYLAN ESTERASE [Trichoderma reesei],1QOZ_B Chain B, ACETYL XYLAN ESTERASE [Trichoderma reesei]
4PSC_A	1.41e-06	20	157	75	198	Structure of cutinase from Trichoderma reesei in its native form. [Trichoderma reesei QM6a],4PSD_A Structure of Trichoderma reesei cutinase native form. [Trichoderma reesei QM6a],4PSE_A Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor [Trichoderma reesei QM6a],4PSE_B Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor [Trichoderma reesei QM6a]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A2J8C362|CUTI1_VERDA	1.01e-16	4	237	3	237	Cutinase 11 OS=Verticillium dahliae OX=27337 GN=VD0003_g7577 PE=1 SV=1
sp|O59893|AXE2_TALPU	1.31e-13	1	230	1	234	Acetylxylan esterase 2 OS=Talaromyces purpureogenus OX=1266744 GN=axe-2 PE=1 SV=1
sp|Q99034|AXE1_HYPJE	4.85e-12	6	213	7	221	Acetylxylan esterase OS=Hypocrea jecorina OX=51453 GN=axe1 PE=1 SV=1
sp|P0A537|CULP3_MYCBO	1.73e-07	3	229	23	226	Probable carboxylesterase Culp3 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=cut3 PE=3 SV=1
sp|P9WP38|CULP3_MYCTO	1.73e-07	3	229	23	226	Probable carboxylesterase Culp3 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=cut3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000227	0.999748	CS pos: 17-18. Pr: 0.9818

TMHMM  Annotations     

There is no transmembrane helices in FOZG_10137-t36_1-p1.