CAZyme Information: PHYSODRAFT_346580-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_346580-t26_1-p1
• CAZy Family: GH28
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
912	JH159155|CGC9	99419.07	5.1646

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsojaeP6497	28142	1094619	1653	26489

• Gene Location: location=JH159155:3476460-3479903(-)

Full Sequence      

MPPHRQHSADFQLQFDLLDDGENRAPSVAQQLPPVAEGCSRLYLCRHGQTDYNMQRKLQG
RGVNMPLNAEGLEQAKSLAKAMKDVPLTAIYSSALKRAFQTADTVAQLHPKIEVQSFGEV
EEMNFGQLEGHPMEMHEDQINTMFKRWEQGEFNAAWPGGESPLDVVARGVSKITEVVSNT
PPKEQVLMVTHGRFNKIVLAQMLHGELNRMTEIHQDNTCVNVIDFDHATQTYHAMALNNI
NHLPGKPGPGGIVAAEYLSRDPNVSVLILEAGPKSMAATGGTDAPDYAKGSGLTKFDIPG
QYDLIMYNPDNEQYRVEWISDAYMWLGKTVGGCSSINSATYFRPPDVYTNQSQWPFPASQ
MNAKMDENEKMHGHTDVPSPDGKWYTQEGYSLVSKALQSLGYSERKLNDPDARNNKHKTF
GHPPFTIRNGQRDSPAAAFWGPMNSRSNVVLLTEAKVDYLVRDKNGKATGVVYNGEYEVR
VSARGAVLMAAGALGTPKVLIQSGVGPNSQLDLLEMVGGFNGIAQGAGRVSNPNVGRNLF
DANLMYVSFSHPEMKSFIFDNTPPEAIDQYMNQSHTGPWAGAGPTLISYESYDVQGRTYD
FQSNVLTHGFGELGQKENAFTIAMYVTNPESRAHPGFDGNGDWRAFNEGDAYFGTPRDLA
AMQSYVQKMVHVLEDQGATFISDTGSDPAAIADFVASTDSYISYFFGGTCYASSDASDME
RCADEKLRVVGLKNVFVADASAMKESTVNPYGFVMYIGREAADQAQSYIASNEGSIDDTC
STLEKDLDFQGEDIGKSYSSSADGCRSICFSMNGCVAFTWTNDNSGTCWLKSGKGTITTK
SGAVSGALKSASSCPALEDDVAEPHGVSMAVKSSDKCCAVCKATGGCKAFTWKEQKGGTC
WLKGGKENKNKE

Enzyme Prediction     

EC	1.1.99.18:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA3	248	763	9.9e-103	0.9434306569343066

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395236	His_Phos_1	9.61e-54	42	227	1	183	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.
225186	BetA	6.46e-41	248	770	16	538	Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only].
223483	PhoE	8.08e-40	41	244	4	206	Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism].
214859	PGAM	3.53e-29	41	192	1	152	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	1.05e-22	41	227	1	143	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
UIZ20744.1|AA3_1	8.19e-228	248	832	37	621
AIG55859.1|AA3_1	3.29e-170	248	903	32	697
AIG55821.1|AA3_1	1.79e-152	248	903	32	701
AIG55820.1|AA3_1	4.12e-134	248	769	32	553
AIG55589.1|AA3_1	4.61e-131	248	747	30	526

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1NAA_A	4.33e-45	248	774	11	539	Chain A, Cellobiose dehydrogenase [Phanerodontia chrysosporium],1NAA_B Chain B, Cellobiose dehydrogenase [Phanerodontia chrysosporium]
1KDG_A	4.70e-45	248	774	16	544	Chain A, cellobiose dehydrogenase [Phanerodontia chrysosporium],1KDG_B Chain B, cellobiose dehydrogenase [Phanerodontia chrysosporium]
4QI4_A	3.52e-34	248	764	16	541	Chain A, Cellobiose dehydrogenase [Thermothelomyces myriococcoides],4QI5_A Chain A, Cellobiose dehydrogenase [Thermothelomyces myriococcoides]
4QI6_A	1.38e-33	248	764	238	763	Chain A, Cellobiose dehydrogenase [Thermothelomyces myriococcoides]
4QI7_A	6.47e-31	248	762	238	760	Cellobiose dehydrogenase from Neurospora crassa, NcCDH [Neurospora crassa OR74A],4QI7_B Cellobiose dehydrogenase from Neurospora crassa, NcCDH [Neurospora crassa OR74A]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q01738|CDH_PHACH	3.32e-43	248	774	243	771	Cellobiose dehydrogenase OS=Phanerodontia chrysosporium OX=2822231 GN=CDH-1 PE=1 SV=1
sp|Q988C9|4PADH_RHILO	1.04e-17	248	774	15	539	4-pyridoxate dehydrogenase OS=Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OX=266835 GN=padh1 PE=1 SV=1
sp|Q7X2H8|CHOX_ARTGO	1.73e-16	235	777	1	538	Choline oxidase OS=Arthrobacter globiformis OX=1665 GN=codA PE=1 SV=1
sp|B1Z034|BETA_BURA4	1.21e-14	248	743	14	509	Oxygen-dependent choline dehydrogenase OS=Burkholderia ambifaria (strain MC40-6) OX=398577 GN=betA PE=3 SV=1
sp|O07617|PHOE_BACSU	3.36e-14	44	245	6	190	Uncharacterized phosphatase PhoE OS=Bacillus subtilis (strain 168) OX=224308 GN=phoE PE=3 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 PHYSODRAFT_346580-t26_1-p1.