CAZyme Information: MGYG000000695_00045

Basic Information

• Species: Prevotella sp000436035
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000436035
• CAZyme ID: MGYG000000695_00045
• CAZy Family: PL11
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1530	MGYG000000695_1|CGC2	165893.41	5.228

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000695	3484843	MAG	Kazakhstan	Asia

• Gene Location: Start: 60268; End: 64860 Strand: +

Full Sequence      

MKKFFVTAALFMLASAGTYAQRFTDKLDRGLVAVQTTKGVYCSWRIQADEYYDVKYNLYR
GGTKVNSEPLNVSNYTDASGSASSKYTVKAVVNGVEQQASKAATVFKSNYKEIKIKHDAS
LKATYEPNDACCADVDGDGEVEILMKFNNKEEGEQLYPKNGPTINGVATKEYSMLACLKQ
DGTVLWWVNCGPNMGDFQNNEQNIVGYDWDMDGKAEVVMRLEEGSTVHMADGTSYTIGAD
GKNGTAWTNYREPKSSGSVEWFTHYGKEFLWYCEGATGKPYQCIEFPLKRLEDGETDLKA
AWGDGYGHRSSKYFFGAPYLDGKHPSIFLGRGIYTRHKFIAYDVDPKTHDLNVRWKWTNN
QPGSPWYGQGYHNYIVADVDWDGRDEIVWGSMVIDDNGKGLSTTGLGHGDSQHIGDFNPY
IHGQEMFACNEDNPSNNYRDATTSKIYYRKTDTNDDGRCLAGNFYNDFPGAVGHSAHDTP
ISTITNDHVSTNTNGLSMNFRIYWDGDLLEECFNDTEVTKPGVGRIAKMEGAYSNNSTKA
TPCYQGDIFGDWREEIIERTADNNIRIYTTTEPTKWRNYSLWYDHQYRNGMVWQPCGYNQ
PPHASYFLGELEGITIAPPPLTTTGREEVSTSIGSSLNGKHAMLDANSDVTVSVANGASP
AIFTDNAPSWVQGTAESECKTKDTEIKYTYYTHTLTGGAFTGSTRLVKQGDGTLVLPNVT
ETYTGKTDVWAGTLQFDGTMESSPVWLNRFAELNSDGGNFKAGIKADYGSVIRPGGKEHV
GTLTTSSLELGFGARVVFDVKDGNIDKVVATKMSIEKKTWENGPQYSAPVFEFASVPEPG
TYTLAEVGELTGNLSDVTVEGLAGKKFSLSYADGKIALTVCASRDSESSTWTGVNGSIWD
LMNTENFSSSDKHFVTGDDVIFDDNASTTSVQLDEEVTPGSVVFKNNSKTYNLSGNGVIE
GDISLSVLGTGTVNITNTNKYSAGTYINGGTLVPSTLANNDGLQYGALGGAGNSINLLND
GTLKTTASMTASHPIILGENGGYLNTTGTLILNGGIKKSNAGSNRNLYKTGAGTLQLNCT
ADYDALYINQGTVYDFQDAHFSGKKVVLNGSKVVLQASNSIYSSNSDNVNIDVPKGKSGI
WYPDGRCDYTGKLTGEGTIDIYGTWIRCPFKGNWSEFAGTINAKRGNKNAYEPVFDFNNS
YGIPLATLNVDSRFTKDYAFCTNGKSFAIGALTGSGYISNGGYFGTGTNTLTIGGKNTNF
EFKGSINGSHVVKNGTGIWTISSESVLANAKSLKIVDGAVKLNKAAATTSMTSPTITYVQ
DAGELRGLGYVYGVNVLAGGNLRAGAATLQTNNTGIITLARNLNVEEGGNIYVNKTKTDP
EYVNPRTGAITQNWAFFKVGGNAIINGTVNVTYKSTWTPMVGEFVKVLECAGTISGNPTF
NLKELPAGMQWDTSKFLAEGLIYVDNATGIDEIGFDGGVFKADVYTLAGFKMTSLQTSQA
TLMKDLKACGLAAGTYIIRTPKGGKKVVLK

Enzyme Prediction     

No EC number prediction in MGYG000000695_00045.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL11	22	629	6.8e-155	0.966996699669967

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10318	RGL11	6.67e-162	25	606	2	564	Rhamnogalacturonan lyase of the polysaccharide lyase family 11. The rhamnogalacturonan lyase of the polysaccharide lyase family 11 (RGL11) cleaves glycoside bonds in polygalacturonan as well as RG (rhamnogalacturonan) type-I through a beta-elimination reaction. Functionally characterized members of this family, YesW and YesX from Bacillus subtilis, cleave glycoside bonds between rhamnose and galacturonic acid residues in the RG-I region of plant cell wall pectin. YesW and YesX work synergistically, with YesW cleaving the glycoside bond of the RG chain endolytically, and YesX converting the resultant oligosaccharides through an exotype reaction. This domain is sometimes found in architectures with non-catalytic carbohydrate-binding modules (CBMs). There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain through a beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
pfam18370	RGI_lyase	3.52e-38	22	105	1	85	Rhamnogalacturonan I lyases beta-sheet domain. This is the beta-sheet domain found in rhamnogalacturonan (RG) lyases, which are responsible for an initial cleavage of the RG type I (RG-I) region of plant cell wall pectin. Polysaccharide lyase family 11 carrying this domain, such as YesW (EC:4.2.2.23) and YesX (EC:4.2.2.24), cleave glycoside bonds between rhamnose and galacturonic acid residues in RG-I through a beta-elimination reaction. Other family members carrying this domain are hemagglutinin A, lysine gingipain (Kgp) and Chitinase C (EC:3.2.1.14).
PRK15319	PRK15319	2.11e-04	908	1083	693	895	fibronectin-binding autotransporter adhesin ShdA.
pfam12951	PATR	2.18e-04	706	734	1	28	Passenger-associated-transport-repeat. This Autotransporter-associated beta strand repeat model represents a core 32-residue region of a class of bacterial protein repeat found in one to 30 copies per protein. Most proteins with a copy of this repeat have domains associated with membrane autotransporters (pfam03797). The repeats occur with a periodicity of 60 to 100 residues. A pattern of sequence conservation is that every second residue is well-conserved across most of the domain. These repeats as likely to have a beta-helical structure. This repeat plays a role in the efficient transport of autotransporter virulence factors to the bacterial surface during growth and infection. The repeat is always associated with the passenger domain of the autotransporter. For these reasons it has been coined the Passenger-associated Transport Repeat (PATR). The mechanism by which the PATR motif promotes transport is uncertain but it is likely that the conserved glycines (see HMM Logo) are required for flexibility of folding and that this folding drives secretion. Autotransporters that contain PATR(s) associate with distinct virulence traits such as subtilisin (S8) type protease domains and polymorphic outer-membrane protein repeats, whilst SPATE (S6) type protease and lipase-like autotransporters do not tend to contain PATR motifs.
TIGR02601	autotrns_rpt	5.80e-04	706	737	2	32	autotransporter-associated beta strand repeat. This model represent a core 32-residue region of a class of bacterial protein repeat found in one to 30 copies per protein. Most proteins with a copy of this repeat have domains associated with membrane autotransporters (pfam03797, TIGR01414). The repeats occur with a periodicity of 60 to 100 residues. A pattern of sequence conservation is that every second residue is well-conserved across most of the domain. pfam05594 is based on a longer, much more poorly conserved multiple sequence alignment and hits some of the same proteins as this model with some overlap between the hit regions of the two models. It describes these repeats as likely to have a beta-helical structure. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIM09959.1	0.0	12	1519	2	1527
AGB29439.1	0.0	19	1529	20	1518
BCS86257.1	2.20e-291	24	895	2	876
ABN51485.1	7.65e-121	22	620	257	814
ADU75030.1	2.01e-120	22	620	257	814

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z8R_A	1.99e-113	20	620	1	578	Crystalstructure of rhamnogalacturonan lyase YesW at 1.40 A resolution [Bacillus subtilis],2Z8R_B Crystal structure of rhamnogalacturonan lyase YesW at 1.40 A resolution [Bacillus subtilis],2Z8S_A Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid [Bacillus subtilis],2Z8S_B Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid [Bacillus subtilis],2ZUX_A Crystal structure of rhamnogalacturonan lyase YesW complexed with rhamnose [Bacillus subtilis],2ZUX_B Crystal structure of rhamnogalacturonan lyase YesW complexed with rhamnose [Bacillus subtilis]
4CAG_A	1.54e-107	22	610	9	577	Bacilluslicheniformis Rhamnogalacturonan Lyase PL11 [Bacillus licheniformis]
2ZUY_A	3.86e-106	21	609	5	590	Crystalstructure of exotype rhamnogalacturonan lyase YesX [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31526	5.09e-113	2	620	12	615	Rhamnogalacturonan endolyase YesW OS=Bacillus subtilis (strain 168) OX=224308 GN=yesW PE=1 SV=1
O31527	1.69e-105	21	609	5	590	Rhamnogalacturonan exolyase YesX OS=Bacillus subtilis (strain 168) OX=224308 GN=yesX 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
0.000297	0.998945	0.000204	0.000174	0.000171	0.000154

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000695_00045.