CAZyme Information: PSURA_74794T0-p1

Basic Information

• Species: Phytophthora ramorum
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora ramorum
• CAZyme ID: PSURA_74794T0-p1
• CAZy Family: GH123
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
774		87294.14	7.5165

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_SC0010:53896-56366(+)

Full Sequence      

MAKDKKKDKLSLSKAVARNRKWLLLLAPLLVVYGLLVMVTTDGGYEDSGGPKSPIRSFLR
HRQTLINGTLHPTSPFYQRGASFDVTVKRDRGVLTCMNNGAIALGVSLIRELRCLGNEEL
IQVYHCGAELSKEFKTLLFNVDNRLELVDVCGDLVELGVMDQDMADKFRNWWIKPLAMYH
TDVRHVMLMDVDDISVKNPAALRDLKPYRKTGTTFFYDRVHSDCYEHVNGQDGDKHYLRK
LFATFDYGRFNVTGGEAPSKHVLGSFAYTGKTCHEMDSSLVLVDKERAGQTVMDIMLWFI
TEERFRFRYSFGDKETFWLAFEMAHVPYSFSPWGVSGVSSTPNRDMEKHPDTLCGSILQY
MPVGDEDPEMLYVNGKALLDAYPEGIDQVPTARWNNMFNSHPTHMTPRLPRTELGSFGDA
ENIYSECLLGLGSTPLPEAFIGSLLRRRLHYWGVQTGMLGTLQHCETKSLLSSSQCPWHH
ISQRCHKEFSSAETMAKHALIVGASAGIGLAVAHKVAPMVDKLTLCSRRCPPDLVASIQA
RNPRLEVVYERLDVSLLHEVRQFTLRHQDTPFDWIVITAGILSLNGRTETKEGLDVKMST
HYYGRFMLVHDLLEGLNRPGVRVLNVLGAGRGGAPHLDDLDLKKSYSIKHCADATTLYSF
VTETHEATKEALSEHAPNASFMHIYPGFVNTGLFNRFPWYVRLPSKAFAAVAAHSPERCA
EYMVATLTKPEFAAGWKLLGERGEVLPKTKYHSDELKHKVWKHTLQTIDTVMEP

Enzyme Prediction     

No EC number prediction in PSURA_74794T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT71	91	341	4.5e-41	0.928030303030303

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
402574	Mannosyl_trans3	2.36e-25	91	330	2	242	Mannosyltransferase putative. This family is conserved in fungi. Several members are annotated as being alpha-1,3-mannosyltransferase but this could not be confirmed.
212492	retinol-DH_like_SDR_c_like	2.09e-20	497	761	2	269	retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs. Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
235627	PRK05854	3.66e-14	497	647	15	170	SDR family oxidoreductase.
187670	LPOR_like_SDR_c_like	7.19e-12	497	732	2	268	light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs. Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
212493	HetN_like_SDR_c	6.60e-10	497	694	1	183	HetN oxidoreductase-like, classical (c) SDR. This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA15193.1|GT71	2.74e-107	39	470	58	520
CCA22801.1|GT71	5.09e-102	19	465	8	430
BAP68847.1|GT71	3.89e-80	91	377	66	358
AIG56397.1|GT71	1.04e-62	69	451	61	454
AIG56246.1|GT71	2.51e-55	91	438	65	437

PDB Hits     

PSURA_74794T0-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1U8QP15|PBCE_EMENI	1.88e-18	499	769	22	328	Oxidoreductase AN1596 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN1596 PE=2 SV=1
sp|E1ACR0|NOTO_ASPSM	1.54e-16	499	691	23	220	NmrA-like family domain-containing oxidoreductase notO OS=Aspergillus sp. (strain MF297-2) OX=877550 GN=notO PE=1 SV=1
sp|A0A097ZPD4|ANDH_EMEVA	3.46e-13	499	696	23	221	Oxidoreductase andH OS=Emericella variicolor OX=1549217 GN=andH PE=1 SV=1
sp|Q8VBZ0|DHRSX_MOUSE	6.41e-10	499	766	46	321	Dehydrogenase/reductase SDR family member on chromosome X homolog OS=Mus musculus OX=10090 GN=Dhrsx PE=1 SV=2
sp|Q8N5I4|DHRSX_HUMAN	1.95e-08	499	766	46	321	Dehydrogenase/reductase SDR family member on chromosome X OS=Homo sapiens OX=9606 GN=DHRSX PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000021	0.000002

TMHMM  Annotations     

Start	End
22	41