CAZyme Information: MGYG000001927_01156

Basic Information

• Species: Prevotella sp900547005
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900547005
• CAZyme ID: MGYG000001927_01156
• CAZy Family: PL1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
397		43447.09	7.5461

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001927	2803818	MAG	Denmark	Europe

• Gene Location: Start: 28580; End: 29773 Strand: -

Full Sequence      

MLVCLFYVFTGNAQLAKQDLNAPFGWANCSSATTGDDYTVTGGGQSENRITLKSTGGDMR
DVISNALKKHDIIVFDGSAGDFMLSSAVDMNELENKTIVGINGARLCTQFYITKDIRTAL
NKANVMKASSSSGTGGTLSNGATIGEERELRTRQALIDFTGDATEAYRKAGILGIKHCNN
IIIRNIKFVGPGSCDLGGSDLISATYTTHLWVDHCDFTDGMDGNFDITNESDFITVSWCT
FSYTKRAYDHMNTNLIGSNDKRYDDAGKLHVTFANCIWGAGCAQRMPMVRFGTVHLVNNY
YDCMGNMAAINPRFSSSVLIDNNYFAPGVKKIFKENDAKAYTFIDNRYTEKFTQPADRGR
VTVPYAYKAVYVADVPGMVTSKYGAGAKLKDPLKIGR

Enzyme Prediction     

No EC number prediction in MGYG000001927_01156.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL1	161	326	1.4e-45	0.7722772277227723

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
smart00656	Amb_all	1.31e-37	161	325	22	186	Amb_all domain.
COG3866	PelB	9.23e-34	1	386	5	342	Pectate lyase [Carbohydrate transport and metabolism].
pfam00544	Pec_lyase_C	6.10e-18	171	325	52	211	Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAW84045.1	1.93e-123	59	397	1	332
ADE83376.1	7.39e-116	10	389	37	421
QVJ81552.1	4.20e-115	10	389	37	421
ABG58437.1	5.05e-52	18	396	20	343
AHJ96631.1	2.72e-51	163	387	127	362

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1VBL_A	2.03e-24	161	386	138	413	Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
5AMV_A	2.90e-18	13	302	1	296	Structuralinsights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168]
1BN8_A	3.32e-18	13	302	22	317	BacillusSubtilis Pectate Lyase [Bacillus subtilis]
3KRG_A	3.91e-18	13	302	1	296	ChainA, Pectate lyase [Bacillus subtilis]
3ZSC_A	5.79e-18	171	301	83	213	Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0CBV0	1.48e-26	175	389	110	325	Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1
B8NBC2	5.42e-26	175	389	111	326	Probable pectate lyase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=plyB PE=3 SV=1
Q2TZY0	5.42e-26	175	389	111	326	Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1
Q00645	6.97e-25	115	366	54	304	Pectate lyase plyB OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyB PE=1 SV=1
Q5AVN4	7.09e-25	173	384	116	322	Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.452995	0.546016	0.000398	0.000240	0.000164	0.000180

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001927_01156.