CAZyme Information: H310_02967-t26_1-p1

Basic Information

• Species: Aphanomyces invadans
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces invadans
• CAZyme ID: H310_02967-t26_1-p1
• CAZy Family: GT71
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
708		79995.01	7.3773

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AinvadansNJM9701	15416	N/A	168	15248

• Gene Location: location=KI913955:1617349-1620031(-)

Full Sequence      

MAAAATPQYAALFRWAHHCDSVSIAGSFNNWGEKFPMEKHADGTFSIALDLAAGLYRYKF
FVDNKAWKYDPDYAFAQDGYGNLNNFITITPAAGDAVQVPIPTMLRGPDLRELPTMNPAA
TIASSEVRKNTTPPVLRPLPPTIRRLSGKHAFPSTPATDAIVQQSPRIKPRSELKKMPPA
LIKRDSIIKPDNAEYGLDETAEAGRTRTPSGGSMTRSKSEESLKALDAGLESRATIVQPA
PKRLSVSHREFSQTSILLAARTEHFGGDLVTQEHQMRQQDGGHRSTLSYPVSMANESQQR
SGKLLIVLVGLPGRGKTFLGHILARHLTWMGHATKVFNVSEYRRTIVKAEVTHHFWDPDN
TSDSQKRAEIGVACLKDALDALANDTCTCAVFDATNASVARRKEIREAAAARPFKYELLF
IESICDDPELIAISINEMKLNSYDYAHFTLDQVVEDYHQRIEHYRDVYMPLEETERCSFI
KIIDVGRQIFCNQVYGYLQSRIMFLMANLQLRPRPIWLSRHGESVYNTQGLIGGDSPLSP
WGVQYAEQLDKFIQAHYPDDTQLSVWTSTMTRTGQTVERIASHGRVVVKWKQLDEIDAGI
CDGMTYEQVAAQYPEEYRARKTNKLHYRYPRGESYQDVIHRLEPVITELMRLDRPVLIVA
HQAILRVLYAYLTNKHPEECPTIDIPLHVVIQITPKAYHCEEVWHHPL

Enzyme Prediction     

No EC number prediction in H310_02967-t26_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396253	6PF2K	7.65e-67	297	513	7	223	6-phosphofructo-2-kinase. This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.
140343	PTZ00322	2.83e-45	280	693	187	622	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
395236	His_Phos_1	1.60e-42	516	703	1	189	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	1.01e-36	516	688	5	180	Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism].
214859	PGAM	1.29e-33	516	668	2	158	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ24287.1|CBM48	6.57e-256	9	708	44	731
BBN14963.1|CBM20	7.66e-93	303	693	397	783
ABO98260.1|CBM48	1.27e-11	9	94	9	98
ARU40701.1|CBM48|GH13_20	1.30e-10	20	93	28	103
BAM83053.1|CBM48	9.64e-10	13	95	316	397

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6IBY_A	2.11e-108	305	700	18	408	Human PFKFB3 in complex with a N-Aryl 6-Aminoquinoxaline inhibitor 6 [Homo sapiens]
6IC0_A	2.11e-108	305	700	19	409	Human PFKFB3 in complex with a N-Aryl 6-Aminoquinoxaline inhibitor 4 [Homo sapiens]
6IBX_A	2.18e-108	305	700	19	409	Human PFKFB3 in complex with a N-Aryl 6-Aminoquinoxaline inhibitor 5 [Homo sapiens]
6IBZ_A	2.32e-108	305	700	21	411	Human PFKFB3 in complex with a N-Aryl 6-Aminoquinoxaline inhibitor 7 [Homo sapiens]
4D4J_A	4.07e-108	305	700	37	427	human PFKFB3 in complex with a pyrrolopyrimidone compound [Homo sapiens],4D4K_A human PFKFB3 in complex with a pyrrolopyrimidone compound [Homo sapiens],4D4L_A human PFKFB3 in complex with a pyrrolopyrimidone compound [Homo sapiens],4D4M_A human PFKFB3 in complex with a pyrrolopyrimidone compound [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O35552|F263_RAT	3.26e-107	305	700	37	427	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 OS=Rattus norvegicus OX=10116 GN=Pfkfb3 PE=2 SV=1
sp|Q5R9C1|F263_PONAB	1.50e-106	305	700	37	427	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 OS=Pongo abelii OX=9601 GN=PFKFB3 PE=2 SV=2
sp|Q16875|F263_HUMAN	1.80e-106	305	700	37	427	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 OS=Homo sapiens OX=9606 GN=PFKFB3 PE=1 SV=1
sp|Q21122|F2612_CAEEL	8.17e-106	305	701	31	429	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase OS=Caenorhabditis elegans OX=6239 GN=pfkb-1.2 PE=3 SV=2
sp|Q91348|F26L_CHICK	1.22e-105	305	701	42	432	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase OS=Gallus gallus OX=9031 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000052	0.000000

TMHMM  Annotations     

There is no transmembrane helices in H310_02967-t26_1-p1.