CAZyme Information: MGYG000002424_01661

Basic Information

• Species: Monoglobus pectinilyticus
• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales; Monoglobaceae; Monoglobus; Monoglobus pectinilyticus
• CAZyme ID: MGYG000002424_01661
• CAZy Family: PL11
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1332	MGYG000002424_1|CGC23	144703.11	4.2809

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002424	2757122	Isolate	New Zealand	Oceania

• Gene Location: Start: 1984200; End: 1988198 Strand: +

Full Sequence      

MKKKLFCVILSIMMLAGCIPAMAVQDGPELNSEIQQSSEQPRQMEKLDRGAFGATAPSGG
VYLSWRLLGSEPMDTVFNIYKNEQKLVDFINNTNYTDLEGSETDKYTIAPVINGQEGEKC
EPITILAGHADKGQESVPYTYFDIPLNIPSPASDYEIVYDSGKSNSPIGGANDVSVGDVD
GDGEYEIILKWDPNNSKDNSQSGKTGRVYLDCYEMDGTQLWRIDMGVNIRAGAHYTQFQV
YDYDGDGRAELAVKTAPGTIDGAGNYVTQAGTTEAIKSADNSASYVNSSGFIIDGPEYLT
IFNGQTGAAMQTVDYDPGRGDTTTWGKTSDKTNRVDRFLACTAYLDGVHPSLVTARGYYG
KAIVVAYDWDGKNLNKRWRCDSTVSGYGSLAGQGNHNVSVADLDGDGCDEIVYGSAAIDN
DGTVAHSTGWGHGDAIHVSDFNNDGKQEIFGVLEEKPNWGTGFRDAAGKETWHFKASGDD
GRGVMDYFSPKYGVLAWDAAFGVRTIGGELISKTTLHDGSYPNFPIYWDGDLYREHFNGD
RISKWNDDTLSFGRLWTIYTNNSVKFINSTKTNPNLQADLFGDWREEIILRHSDNSALRV
FASISPTDYKFTTFMHDSQYRSAIAWQNTAYNQPPHQSYYIGYDKDVSEYVQPNLYYAPL
PESVVTVKDSSGNLLSGASVKIDSQIMTTDENGMVSARLLPGTHNYEVELDRYILSKGAF
EVPENSGAALEVVLEAKQYIYDSSNDETGSKFVYDGSEGAALTFSSSKEWQFTQDSSDGG
RSFKADFETAYGGNAELEFAFGTGGTKDAGGAWNWTGRAYTYEIKLLDSTEKTVLAIGQE
YSESGANEAYYYSGTGAKTNISSGTVFGSPNITKRSSSNWRIKISLDLTNGTAKLILSDD
SGENGYIIENISIDSADFSSLEIGSIASSNVTWSPKVKDVLYWADSVTPPSPPPTLDPTK
PTPTAKPTAEPTATPLPTDAPIIGQSWDFDNLKAGDIYGNSDDNNTISNNNGKSINIDFG
TSAADGAVPPAITQRAEGNNYIQFTDKGAGQDGWSYLPETVLDGDKIIFEEDFMSGDTAK
DTPLFRIFDSNNANPDNTYTTAKDGRVFEVMTVEGGTLKLNDYFSMGASATKPKDTQISG
FSFSPNKWYSLKLEYTKSDNKVKVYTKEADSSDYTLRGTVTLGSGTKKIDEVPQLLPTKV
QCSTRGSSANSLGIDNITVGVQGGSEVPEVTPTVQPASEFMYTLNSIAEAENGININLTK
NKEGIGSNVIIAAAYDRETGALTAVETSDITMNVGDSSNIFVPLAVSETNEIKVFVWNST
DGIEPLSKSISK

Enzyme Prediction     

No EC number prediction in MGYG000002424_01661.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL11	42	649	4e-225	0.9879931389365352

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10318	RGL11	0.0	44	639	1	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	3.33e-25	42	125	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).
cd11308	Peptidase_M14NE-CP-C_like	0.002	667	728	6	69	Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain. This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.
pfam04886	PT	0.004	960	983	9	36	PT repeat. This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUO19809.1	0.0	1	1332	1	1332
AIQ75296.1	4.71e-178	37	659	2	589
AWV36810.1	8.61e-178	37	659	20	607
QEY11698.1	2.46e-175	42	680	50	658
ALP35944.1	4.74e-174	18	656	12	619

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z8R_A	7.47e-169	42	656	3	581	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	9.42e-168	37	656	4	588	Bacilluslicheniformis Rhamnogalacturonan Lyase PL11 [Bacillus licheniformis]
2ZUY_A	7.78e-162	42	642	6	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	1.06e-167	42	656	40	618	Rhamnogalacturonan endolyase YesW OS=Bacillus subtilis (strain 168) OX=224308 GN=yesW PE=1 SV=1
O31527	3.29e-161	42	642	6	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000396	0.454928	0.544077	0.000203	0.000205	0.000190

TMHMM  Annotations     

start	end
5	24