CAZyme Information: MGYG000001543_01543

Basic Information

• Species: Lachnoclostridium sp900078195
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium; Lachnoclostridium sp900078195
• CAZyme ID: MGYG000001543_01543
• CAZy Family: PL11
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
3704		403221.64	4.229

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001543	4599950	Isolate	not provided	not provided

• Gene Location: Start: 820379; End: 831493 Strand: -

Full Sequence      

MSWGRKLKQKKVLKKVQTLILVTTLTVGCIQTPMNVSAANSFKGEMSNAISSVLDAMDKK
GEYDNAVEALNSSLTSLEGAASVTGLMVTDTQEDSVTIEWDPFEADNLVGYNVYWADKDT
ATQVFMKLTKDGIKTMDNELITVGPETTSFTFHKSTHVNHYFKVSPVFETGEGSKSEVIK
TQTAKEYSAYLENLDRGLMKVATTEGVFLSWRLLGTEVDGYSETGLTGTDFNVYEGENLL
ATVSDSTNYVVAGGSINSSYYVVPVVDGIEVIENRSGEATKMDAMDGAGYLEIPLQIPHD
TTIEEVYGISSEEITLLNSPRTDTYTTNKITYSANDVSVGDVDGDGEYEFFVKWDPSLSK
DVSQQGYTGKQYIDCYKLDGTLLYRIDLGINIRAGAHYTQFLVYDFNEDGKAEISLKTAP
GTKIIKFNNNNQDEIASETYITTPDGESNEADYVFTAAEYREYLIQMFMDWGVWANDSED
MIEAKANWDKNLIKLFAPEDDMVSIVTEADGKYTVKKVSREEAGYTADDLIVNVPVRDAN
GEVVYQSSGVANAYMRTVLFDDEATGLTASMNHEGGYTLEEATALADYFLNGYQYRMKKH
DLNYYEGYIITGSEYLSVFDGETGAELDTIMYEFERQDDGMLWGDYAMNYMEPGNRCDRF
LSTVAYLDGENPYMVIGRGYYTRSTIATYTLTEDGKLELHWTIDSGWTVMTNPFNDGPHG
MNGNNTNVGTNGISFSLFSGQGDHYISAADVDGDGCQEIIYGGAIVDHNGDLYSSGGDYV
NGGAWAKYGHGDSIHVTDIDPDRPGLEIFSCFEGGPGAPYGTALRDAELNTVIPGFQSVY
TGVDTGRCMIGDLLPNVRGFELWGVNTTDAKGNIVSVNTIGTNQNIYWAADRTTQIYTGN
IVKANGTSATTMLTATGTTSNNGTKGNASLIADVFGDWREELIARTSDNTALRIYTNTEV
STTKLYTLMHDTQYRTNVAGQNTAYNQPAYTSFYLASDMDFEYVPIPNVKKEQEPGATEI
APSRVILDKTSLTLKVGGKIALTATVLPNKATNKTVSYTSSDEAVAVVDKDGVITGIKKG
ISTITVSTINGKTATCKVIVKDGYSEVGLDEFAIGETKTFTFGSTKVKDTITVGAATEYT
SESKYGWQNATSISLTESADYVTGNNVRTVDGTNVIYDYPTFNVDLPVGFYEVTIVQGSD
AEDTVNGAYVEGNMYSVRWSTQGFSTSFTEPSESSYIVTPKGTTKESKVLTAVADGTLTI
QLATSLNDEGESGVVSIRSISITRVASNVEESVNPTLRFIGDSTVATYPPEDGNEWTPIP
ERTGWGANFAMARFMSDEVELVNKAVAGSSIKSYLADGYYNDFFLTARPGDTVIIEGGIN
DSAAGRRYSDATSYEAYLRYYIESCQTFGLDVVLSSGTSSATTYTDVMVKLAKEYELTYI
DLLGEFSNYKNKISQTAQGDLTVDGTHLSRVGAVLAAQIVAGHLAQIEGLSISGYVKSQD
INNNAPTAVVTGVNVKAQTSNSVTLSWNIDEETLYEPNQLVTRFNIYRKEKGAANSSYTK
VSQSRAYVSASMTAPKLQATIESPVVGDYDYAIAVVGLVGEGPKSESITVTEFKPDTTYQ
LLELMEQYEEQMYDSTHYTAESYINLRTAFHRASTALEVNAPEEELAEILLAVKAAVEGL
VRVNTVVMEEDFEAETIGSKWGTTGHQLLSVIMEEDGNHLANAYVEAAGTRQIKKEITGA
VSELLSVEFEWYPGQPDRRNCTEIQFSDAKGVYFSLKTSNNGHIGYVVGAYDSNSTAYLT
GDGFHAENTQATDCGLSNEVWYNVRIVFDYKNHTADLYLIPRDDESLPSKVIKGIEISKE
ASQVSLMNFLCMRGKQDNGSSNDLSVLWDTYLDNFAIYYVINKEEADLTTFHQTKDVYQG
KIQGISADSLTAEEFVRAETAIELVDNNVGFMTQEDVNYLVSVMEEAVAAVPERTAVKAI
TLPSEISITAGLVQTVVAQLEPLNANELLTWSSANEDIAVVSYDGKTAVIRGIKEGSTEI
TVRSQGNVSAVVKVNVVGSAYLFGNGQRISADSFYVNGIGFNNFTYKTAAMGWVDGIYHP
RELTKEAGTSYINVEESTNDYLAINSVVWSENGGDRDEDTIVYENTSAFDLDLAHGNYTV
SVNFINPTKNAMNVVVKAEDITRYASGDHGETELAKATVLAGQTKTVSFEIALMDDSLTL
RFEQDAVASSLNSAAVKTVYVKSVSVVATEEKKTEEVPTIFLLGDSTVQTYTKANYRTGW
GQVFYTALSGASDDSIVEETSEGYAYYKTDLTAVKNYARDARSAKSFLQEGRLNEVLLNV
KEGDYVLAQFTHNDSNTARPNRYLSTEDFKTYLLNYKKAVEERGATFVLVTPIVINAIEN
GKWDHRFESYRQVMLELGLSEQIPVLDLMGASYSLVNEMGQSAVNALGMYMSDTVHLQKN
GAMMYTQLLANLIHSYDMDDQLATLKAALKKVDASVTFDQSKISLQPQKSVSLAYQTTGL
DGKTATYYTSDPSVATVDSNGAVTGVSKGNAIITISIANGADTATTDCTVYTDYCLVEVA
GEQTVNEQSVKEPSVSELLLSEQTESENTFSLMSASLTNLTSSILESDLSDVSNEELSLF
ALESTGNVVVDPDVTVEDMDTQAIYKFDFGNKSGFASGYTPITNGKYNEETGYGFISDIS
LINYSSLSTGVASKDGATDDEIALYTACQDAVRGSALEFVVDVPAGTYMVSLYANVSWNL
DMYKASTYSINGYSVGGIVSEETTTDNIAKNVKVTLTEPGQIVIRGTNPGKLAIFNALVI
SKYVPAVKTYNEAAWNELKHTSARLNIKLGLLADNTTPLEFDTSLITKMTAMKRALKVVK
GMPVADYATGDEAMAKAVEAMENKTLYTESSIEKLETAVAELQAVIDSLENVDQAVVTAL
SVIDYWLLGVEVEDIVEPYDLYVDFDVPSTSVEYLTDGYTSVLNTSTYSELLGYGLVTAS
NGRNRGTGNSLFDDFVMNTAFLVDVPAGNYMVRAYCGDLMTGCNNTSVINIIDTTTNEAL
VVDATTRSAGEEISFIDMYFEVKESTQIRVEVSGRLNALLVEQIVNVSVAEIDIAKLIDL
VNTIDAAGLIETNYTISSYQALVKALEEAREAIDKGVSYVQEYEKLLNSLISAYEGLKVR
EVAHEILIDFGTETSAVSTDSKFEGDGGIATLGTNVLQGLGTMVYTENSLDNGQHFGFDR
VMPANETSSGGAYFRDYVYSKGGVPYTFYADMPVGTYYVYVYTGDKLSNNTTKLYFNNGE
AVITSNTAVEVVSGGAVSGSAIASVSGCAIYSQTSSGGGQYSAPACIYTVDVVESDTISS
IDGIKMGRFSITLFDDTATSADAVTARLNGIELTPVNKPEPTPTPEVSPTPTEKPTPTEK
PIPTVEPTPTEKPIPSVEPTPTEKPIPSVEPTPTEKPIPSVEPTPTAKPTPSVEPTPTEK
PIPSVEPTPTAKPTPTTEPTYTPDPEPTVTPEPDVLKDIILREEEITLYVGGTIENERWI
PIKLPENVKKVTSFDSKVLNKLKGDIVPVTIKYSSDNESVAVINHVGRIFAVGEGTSKIT
ATITQKNGTSKDFVIIVKVMKAYIEIVSQSNVINIGEKVPFEVKVYGLRKEDIRWSTSKV
KRAMVAMNLGKEKVMVYGKSAGTDYVVIKCGTISKAIKVIVVKK

Enzyme Prediction     

EC	4.2.2.23

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL11	596	1018	1.1e-126	0.6270627062706271
PL11	191	460	1.1e-69	0.3876500857632933
CE12	2259	2471	1.3e-45	0.9857142857142858
CE12	1298	1483	2.2e-24	0.9809523809523809

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10318	RGL11	0.0	191	993	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.
cd01821	Rhamnogalacturan_acetylesterase_like	3.12e-46	2258	2473	1	198	Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
cd01821	Rhamnogalacturan_acetylesterase_like	4.76e-25	1295	1481	1	195	Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
pfam18370	RGI_lyase	1.69e-23	191	271	3	77	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).
NF033839	PspC_subgroup_2	5.67e-14	3395	3517	374	483	pneumococcal surface protein PspC, LPXTG-anchored form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAB04833.1	7.69e-238	83	1010	37	845
ALA52488.1	5.11e-228	79	1027	31	859
BAD62935.1	1.76e-227	79	1027	31	859
AST95272.1	2.56e-227	79	1012	31	844
QNM41625.1	2.56e-227	79	1012	31	844

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4CAG_A	1.95e-123	191	999	11	579	Bacilluslicheniformis Rhamnogalacturonan Lyase PL11 [Bacillus licheniformis]
2Z8R_A	1.64e-115	191	1009	5	580	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]
2ZUY_A	2.71e-109	191	999	8	593	Crystalstructure of exotype rhamnogalacturonan lyase YesX [Bacillus subtilis]
2O14_A	5.64e-12	1181	1497	79	369	X-RayCrystal Structure of Protein YXIM_BACsu from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR595 [Bacillus subtilis]
1DEO_A	1.21e-06	2259	2462	2	201	RHAMNOGALACTURONANACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.55 A RESOLUTION WITH SO4 IN THE ACTIVE SITE [Aspergillus aculeatus],1DEX_A RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.9 A RESOLUTION [Aspergillus aculeatus],1K7C_A Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution [Aspergillus aculeatus],1PP4_A The crystal structure of rhamnogalacturonan acetylesterase in space group P3121 [Aspergillus aculeatus],1PP4_B The crystal structure of rhamnogalacturonan acetylesterase in space group P3121 [Aspergillus aculeatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31526	2.12e-114	191	1009	42	617	Rhamnogalacturonan endolyase YesW OS=Bacillus subtilis (strain 168) OX=224308 GN=yesW PE=1 SV=1
O31527	1.18e-108	191	999	8	593	Rhamnogalacturonan exolyase YesX OS=Bacillus subtilis (strain 168) OX=224308 GN=yesX PE=1 SV=1
O31528	1.53e-21	2260	2470	5	199	Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
O31523	5.91e-16	2260	2470	8	209	Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
P42304	4.40e-12	1108	1484	19	374	Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2

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
0.000532	0.462645	0.536067	0.000293	0.000250	0.000191

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001543_01543.