CAZyme Information: PHYCI_86129T0-p1

Basic Information

• Species: Phytophthora cinnamomi
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
• CAZyme ID: PHYCI_86129T0-p1
• CAZy Family: GT22
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
541		58513.90	4.1432

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_SC0180:59912-61537(-)

Full Sequence      

MLAGHLASAILLFASTFVATVNAASDFGYTSSSGSWVITSGDGLTITMDQDTCDITSMLL
NDSELQYSAKNTHVNSGLGTVTSSLKKLDDSTIQITCKTTGLEQTYLFRPNENAIYMSTY
HTTDLALAELRFLARLDRTVVDNAMLNASDTVGMSAIEASDVYADDDGVTASKFYSGIPF
IEDRVHGVTSDAGGVYFIMSDYAYEKSVGGPFFRDINNKFDVANELTFYMFSDHTRTEDY
RYGFHGPYALVFTDGNTPSTSDVDFDFFQDLDLTGFTTETERGTMTGIITDSSNVLGSSD
VVVAFSNDDAQYWVSVASNASTFTSPLMRPGTYNATIYKKQLAVSSDLVVVTQGSATKQT
LEVTYELESSPVWRIGEWDGTPDGFLNAANIHKMHPSDSRLDTWAESLTFTPGTDDDSTF
PMAMFRAVNDPITLSFTLTSAQAAEARTLKIGLTLAQSSGRCSVTVNSDWTAKVLASVAV
STRGVTRGVTLGNYKLYEYTIPTSALVAGANKIELSIASGSTDPSEEWLSASVVFDALEL
V

Enzyme Prediction     

EC	4.2.2.23:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL4	24	530	1e-160	0.9939879759519038

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
401282	RhgB_N	9.72e-125	27	275	1	251	Rhamnogalacturonan lyase B, N-terminal. Members of this family are found in both fungi, bacteria and wood-eating arthropods. The domain is found at the N-terminus of rhamnogalacturonase B, a member of the polysaccharide lyase family 4. The domain adopts a structure consisting of a beta super-sandwich, with eighteen strands in two beta-sheets. The three domains of the whole protein rhamnogalacturonan lyase (RGL4), are involved in the degradation of rhamnogalacturonan-I, RG-I, an important pectic plant cell-wall polysaccharide. The active-site residues are a lysine at position 169 in UniProtKB:Q00019 and a histidine at 229, Lys169 is likely to be a proton abstractor, His229 a proton donor in the mechanism. The substrate is a disaccharide, and RGL4, in contrast to other rhamnogalacturonan hydrolases, cleaves the alpha-1,4 linkages of RG-I between Rha and GalUA through a beta-elimination resulting in a double bond in the nonreducing GalUA residue, and is thus classified as a polysaccharide lyase (PL).
199905	RGL4_C	1.24e-47	373	541	1	161	C-terminal domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
405384	CBM-like	2.96e-45	371	540	1	157	Polysaccharide lyase family 4, domain III. CBM-like is domain III of rhamnogalacturonan lyase (RG-lyase). The full-length protein specifically recognizes and cleaves alpha-1,4 glycosidic bonds between l-rhamnose and d-galacturonic acids in the backbone of rhamnogalacturonan-I, a major component of the plant cell wall polysaccharide, pectin. This domain possesses a jelly roll beta-sandwich fold structurally homologous to carbohydrate binding modules (CBMs), and it carries two sulfate ions and a hexa-coordinated calcium ion.
199907	RGL4_N	1.03e-38	27	261	1	265	N-terminal catalytic domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold; the middle and C-terminal domains are both putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
405387	fn3_3	3.86e-12	282	358	2	74	Polysaccharide lyase family 4, domain II. FnIII-like is domain II of rhamnogalacturonan lyase (RG-lyase). The full-length protein specifically recognizes and cleaves alpha-1,4 glycosidic bonds between l-rhamnose and d-galacturonic acids in the backbone of rhamnogalacturonan-I, a major component of the plant cell wall polysaccharide, pectin. This domain displays an immunoglobulin-like or more specifically Fibronectin-III type fold and shows highest structural similarity to the C-terminal beta-sandwich subdomain of the pro-hormone/propeptide processing enzyme carboxypeptidase gp180 from duck. It serves to assist in producing the deep pocket, with domain III, into which the substrate fits.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA68112.1|PL4_1	8.95e-124	27	540	23	522
QRW20454.1|PL4_1	3.40e-121	27	540	22	513
BCS11429.1|PL4_1	1.04e-120	26	540	21	526
UJO24073.1|PL4_1	1.05e-118	27	540	21	530
BAM14847.1|PL4_1	5.81e-117	11	540	6	526

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1NKG_A	2.16e-115	27	540	2	506	Rhamnogalacturonan lyase from Aspergillus aculeatus [Aspergillus aculeatus]
2XHN_A	1.71e-114	27	540	2	506	Rhamnogalacturonan lyase from Aspergillus aculeatus K150A active site mutant [Aspergillus aculeatus],2XHN_B Rhamnogalacturonan lyase from Aspergillus aculeatus K150A active site mutant [Aspergillus aculeatus],3NJV_A Rhamnogalacturonan lyase from Aspergillus aculeatus K150A substrate complex [Aspergillus aculeatus]
3NJX_A	6.79e-114	27	540	2	506	Rhamnogalacturonan Lyase from Aspergillus aculeatus mutant H210A [Aspergillus aculeatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q2U0Q1|RGLA_ASPOR	5.79e-117	11	540	6	526	Probable rhamnogalacturonate lyase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=rglA PE=3 SV=1
sp|B8NCU7|RGLA_ASPFN	8.17e-117	11	540	6	526	Probable rhamnogalacturonate lyase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=rglA PE=3 SV=1
sp|Q5AX45|RGLA_EMENI	3.51e-115	27	540	22	525	Rhamnogalacturonate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=rglA PE=2 SV=1
sp|A2R2L1|RGLA_ASPNC	5.59e-115	26	541	21	526	Probable rhamnogalacturonate lyase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=rglA PE=3 SV=2
sp|Q00019|RGLA_ASPAC	1.97e-114	27	540	21	525	Rhamnogalacturonate lyase A OS=Aspergillus aculeatus OX=5053 GN=rglA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000217	0.999730	CS pos: 23-24. Pr: 0.9790

TMHMM  Annotations     

There is no transmembrane helices in PHYCI_86129T0-p1.