CAZyme Information: PHYCI_297794T0-p1

Basic Information

• Species: Phytophthora cinnamomi
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
• CAZyme ID: PHYCI_297794T0-p1
• CAZy Family: GH43
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
908	PcinCBS144-22_SC0001|CGC1	98821.11	6.3973

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcinnamomiCBS144-22	26201	1048749	70	26131

• Gene Location: location=PcinCBS144-22_SC0001:1129145-1132649(+)

Full Sequence      

MPPHRQHSADFQLQLDLVNDENNTRSVAQQLPPVAEGCSRLYLCRHGQTDYNMQRKLQGR
GVNMPLNAEGLEQAKCLAKAMKDVPLTAIYSSALKRAFQTADTVAQLHPKIEVQAFHDIE
EMNFGQLEGHPMELHEEQISTMFKRWEQGEFNVAWPGGESPLNVVARGVSKITEVVSNTP
PKEQVLMVTHGRFNKIVLAQMLHGELNRMTEIHQDNTCVNVIDFDHATQTYHAMVLNNIN
HLPGPPGPGGLVAAEYLSRDPNVSVLILEAGPKSMAATGGTDAPDYAKGSGLTKFDIPGQ
YDLIMYNPDNEQYRVDWVSDAYMWLGKTVGGCSSISSVTYFRPPDIYTNQSQWPFSASQM
NAKMDENEKMHGHTDVPSPDGKWYTQEGYALVSKALLSLGYSKRTLNDPDARNNKHKTFG
HVPFTIKNGQRDSPAAAFWVPMSTRSNVKLLTKAKVDFLVRDAKGKATGVVYNGGSQALV
SARGAVLMAAGALGTPKVLIQSGVGPNSQLDLLEKIGGYPGISQDAGRVANPNVGRNLFD
ANLMYVSFSHPDMKSFIFDNMPPDAISQYMNKSHTGPWAGAGPTLISYDSYEVQGRKYDF
QSNVLTHGFGELGQKKNAFTVAMYVTNPESRAHSGFDVNGDWRAFNEGDAYFGTPRDLAA
MQSYVQKMVRVLEDSGATFISETGSDPAAVADFVASTDSYISYFFGGTCYVSSDASDIER
CADEKLCVVGLENVFVADASAMKESTVSPYGFVMYIGREAADQAKRYIASNKGSTDDTCL
PLENDVDFQGGDIGQSHSSSADRCCSICSSTSGCLAFTWTNYNRGTCWLKSGKGIIKTKS
GAVSGVLKSASSCPALEDNVAEPHGVTMIAKSSEKCCSVCKATGGCKAFTWKDQNGGTCW
VKGGKENK

Enzyme Prediction     

EC	1.1.99.18:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA3	247	762	5.3e-97	0.9434306569343066

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395236	His_Phos_1	2.17e-54	41	226	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.
223483	PhoE	1.43e-40	40	242	4	205	Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism].
225186	BetA	8.26e-31	252	769	21	538	Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only].
214859	PGAM	8.64e-29	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	3.49e-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	4.31e-232	247	847	37	637
AIG55859.1|AA3_1	3.45e-172	247	902	32	697
AIG55821.1|AA3_1	1.39e-154	230	902	23	701
AIG55820.1|AA3_1	3.40e-131	247	757	32	542
AIG55589.1|AA3_1	9.74e-129	247	746	30	526

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1NAA_A	7.71e-42	247	761	11	531	Chain A, Cellobiose dehydrogenase [Phanerodontia chrysosporium],1NAA_B Chain B, Cellobiose dehydrogenase [Phanerodontia chrysosporium]
1KDG_A	8.31e-42	247	761	16	536	Chain A, cellobiose dehydrogenase [Phanerodontia chrysosporium],1KDG_B Chain B, cellobiose dehydrogenase [Phanerodontia chrysosporium]
4QI4_A	3.49e-34	247	763	16	541	Chain A, Cellobiose dehydrogenase [Thermothelomyces myriococcoides],4QI5_A Chain A, Cellobiose dehydrogenase [Thermothelomyces myriococcoides]
4QI6_A	1.36e-33	247	763	238	763	Chain A, Cellobiose dehydrogenase [Thermothelomyces myriococcoides]
4QI7_A	5.96e-30	247	761	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	4.37e-40	247	761	243	763	Cellobiose dehydrogenase OS=Phanerodontia chrysosporium OX=2822231 GN=CDH-1 PE=1 SV=1
sp|Q988C9|4PADH_RHILO	1.29e-16	247	772	15	537	4-pyridoxate dehydrogenase OS=Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OX=266835 GN=padh1 PE=1 SV=1
sp|Q6D6D9|BETA_PECAS	5.13e-15	247	766	11	531	Oxygen-dependent choline dehydrogenase OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=betA PE=3 SV=1
sp|P0DO29|ERIK_HERER	1.72e-14	247	579	42	385	Dehydrogenase eriK OS=Hericium erinaceus OX=91752 GN=eriK PE=3 SV=1
sp|A4JJG6|BETA_BURVG	4.84e-14	247	548	14	307	Oxygen-dependent choline dehydrogenase OS=Burkholderia vietnamiensis (strain G4 / LMG 22486) OX=269482 GN=betA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000061	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PHYCI_297794T0-p1.