CAZyme Information: PSURA_96418T0-p1

Basic Information

• Species: Phytophthora ramorum
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora ramorum
• CAZyme ID: PSURA_96418T0-p1
• CAZy Family: PL3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
903	PramPr-102_SC0076|CGC1	97961.40	5.1003

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PramorumPr-102	15743	N/A	251	15492

• Gene Location: location=PramPr-102_SC0076:117021-120558(+)

Full Sequence      

MPPHRQHSDFQLQLNLVENGEAKSLTISQQLPPVAEGCSRLYLCRHGQTDFNMQRKLQGR
GVNMPLNAEGLDQAKCLAKAMKDVPLTAIYSSALKRAFQTADTVAQLHPKLEVQPFTEVE
EMNFGQLEGHPMEVHETQINLMFKRWEGGEFDAAWPGGESPREVVARGVKKINDVISSTP
PKEQVLMVTHGRFNKIVLAQMLHGDLTQMTDIHQDNTCVNVIDFDHATQTFHAMALNNID
HLPAPPAQTFDVIVVGSGPGGLVAAEYLSRDPNVSVLILEAGPKSMAATGGTDAPDYAKG
SGLTKFDIPAEYDLIMYNPENEQYRVDWVTDAYMWLGKTVGGCSSINSATYFRPPDSYTN
QSQWPFPASQMNAKMDENEKMHGLTDVPSPDGKWYTQEGYSIVSKALKSLGYDERALNDP
VARNSKHKTFGHTPFTIKDGKRDSPAASFWGPMSTRDNVQLLAEAKVDFFVRDSAGKATA
VVYNGGSQVFVSDRGAVLMAAGALGTPKVLIQSGVGPSAQLDLLEKIGGYHGVTQDADRV
INPNVGRNLFDANLMYVFFSHPDMKSFVFDNRPKEAVDQYMNKNHTGPWAGAGPTLISFE
SYDVQGRTYEFQSNVHTHGFGGLGDQEDAFTIAMYVTNPESRAHSGFDSNGDWRAFNEGD
AYFGTPRDLAAMQSYVQKMVRAMEENGATFISESGSDPAAVADYVASTDSYISYFFGGTC
YASSDASDTERCADEQLRVVGLKNVFVADASAMKESTVNPYGFVMYTGREAADQAKSYID
SNAGSNGSDIGSTPSKSADGCCARCSDTTGCTAFTWTDNNGGSCWLKSGKGAIKTKSGAV
SGVLKIATSCPALEDNVAEPHGVTFAANSSDKCCSVCKATGGCKAFTWKDGTCWLKGGKE
NEE

Enzyme Prediction     

EC	1.1.99.18:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA3	245	773	7.5e-109	0.9671532846715328

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395236	His_Phos_1	7.03e-55	41	237	1	194	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	1.95e-42	243	780	1	538	Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only].
223483	PhoE	1.74e-41	40	246	4	206	Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism].
214859	PGAM	3.85e-28	40	191	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	5.01e-23	40	226	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	1.83e-232	250	844	29	637
AIG55859.1|AA3_1	1.80e-166	249	896	23	697
AIG55821.1|AA3_1	8.57e-155	249	896	23	701
AIG55820.1|AA3_1	9.75e-141	247	768	21	542
AIG55589.1|AA3_1	2.59e-135	247	757	19	526

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1KDG_A	1.50e-49	243	784	1	544	Chain A, cellobiose dehydrogenase [Phanerodontia chrysosporium],1KDG_B Chain B, cellobiose dehydrogenase [Phanerodontia chrysosporium]
1NAA_A	8.55e-49	250	784	3	539	Chain A, Cellobiose dehydrogenase [Phanerodontia chrysosporium],1NAA_B Chain B, Cellobiose dehydrogenase [Phanerodontia chrysosporium]
4QI6_A	2.16e-37	134	774	118	763	Chain A, Cellobiose dehydrogenase [Thermothelomyces myriococcoides]
4QI4_A	4.23e-37	243	774	1	541	Chain A, Cellobiose dehydrogenase [Thermothelomyces myriococcoides],4QI5_A Chain A, Cellobiose dehydrogenase [Thermothelomyces myriococcoides]
4QI7_A	3.46e-35	228	772	208	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	1.56e-47	243	784	228	771	Cellobiose dehydrogenase OS=Phanerodontia chrysosporium OX=2822231 GN=CDH-1 PE=1 SV=1
sp|Q988C9|4PADH_RHILO	1.55e-20	245	773	2	531	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	1.03e-17	234	777	1	528	Choline oxidase OS=Arthrobacter globiformis OX=1665 GN=codA PE=1 SV=1
sp|Q9WWW2|ALKJ_PSEPU	1.40e-17	250	753	2	504	Alcohol dehydrogenase [acceptor] OS=Pseudomonas putida OX=303 GN=alkJ PE=3 SV=1
sp|Q00593|ALKJ_PSEOL	3.11e-16	250	753	2	504	Alcohol dehydrogenase [acceptor] OS=Pseudomonas oleovorans OX=301 GN=alkJ PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000015	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PSURA_96418T0-p1.