CAZyme Information: MGYG000001332_01161

Basic Information

• Species: Massilioclostridium methylpentosum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Massilioclostridium; Massilioclostridium methylpentosum
• CAZyme ID: MGYG000001332_01161
• CAZy Family: CBM66
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1704	MGYG000001332_11|CGC7	183164.53	4.2317

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001332	3406391	Isolate	not provided	not provided

• Gene Location: Start: 1422904; End: 1428018 Strand: -

Full Sequence      

MMLKQGMKRILALVLSVAVAGAVLVSPLSASAQQGTTAPGAPYGLLTNELEHPLNVETPT
FSWWLEDADVDEGQTAYQLVVRDELTGEVVWDSGKVESSEQSNVPYGGDALSPAHPYTWT
VTTWDSKGLQSPESEPAAFATGLADADWNADWIQKPNLPITVESSGAAAHVEGGGLTIYS
EGTDWADYKMNVEACAKQGAAGIVLRAQDEDNAYIWALVPGTGLTKTALVNGEAKDLGTV
AFDVVEGAYYSVEIVADGSTITTKIDGQLIDTTTDSTFSAGTVGFYEADGQAGDFQKLSV
TSLARVVDSIYVAGGSNENSQIVLNDKGYDWSDYILDFDMQINDTSNDATALVLRASSDY
KTGYMWQFTRKKGGLARHTRTNGKFNKLDGDGAVPYSFKANTYYHITISLIGNTITTSVN
GEVIDTYVDTANVASKGTFGFRNASGEGGTYANLKVTAPDGTPIYTEDFLDLSRFKFLDG
NAANTITAKDNTVTYLSPDFSKGFEGWSNSSSMSTADGSNWATSTSSGITLAKTGKDWDN
YTLTTRIIAKTGAAGVMFRTTDAQSGYMWQIVPGTGLKVHKQVNGKFTTLKNPIPCDIKA
GQTYRMTINANGSVIKTYINGQLVDITDDNTYATGTVGFRQSTTGNEVGQFSDVMVLDAS
GEVLFQDNFTNGLGQWDISTTTAAKGSNLYWYARTEQPLEEGKTPVRALAYMAAAHDYEL
SVNGTRIGRGQSFDYSSETHYQGWDITEALDGSGTIAVGVLARWYGNGQGRAGGTQGLLG
QIVVYYDDGSTQVISTGKDWVAEEAPLSGSTKRNGEGDFVEEYDARKAIADYSAVGLDVS
GWMPVHVLGAHPADPFTNVEPELSHVTEETMSPVSVEKLSDGTTLVDFGRVIPARLSVDF
KNGVAGRKITLQTGYELKDNGRINTSSSATQSTNMTFIYTQTEGAQRYDTWDHLAFRYLE
IPASAGETFTVQDITATLLYAEVPEGRDSTFTSSNEMLDAVYDFMKISALYSAQNQFVDT
PTREKGQFLQDSINIGAVTTTSWYERETSRKAIRQFLDSADRYWNSGGDLGHYNSVYPNG
DGKRDIPDFSLNVPIWIWRYYQQTGDREILEYAYPYLQNTADYAYNAIPTEGATAGLVTT
LPGGSGDYKNGIVDWPKPGRFDYDMSTAARTTVNALSVRVFDTVAEIAKELGKDDSEVAV
YADRAANLRQAMNEKLITEDGVYCDGLLSDGTQSKHNGQHSTSYAIAFDIAPADKVEAMA
DYVASLGMKQGPMTADILVEALFDADRADAVLNLMTNTDDLGWAKLIADGNTFTWEQWVH
GQSQSHGWGAASAPLILENFLGVKVTTAGAKTVTIDPARDVLEHAAGRVVTERGAVDVSY
SGTGTDYTLKVTVPVNMQAEVVLPKLEGGQFVDKNGNSGTSSFTEDEQIVTVGSGTREFV
FQTYVDANKAILNAVISYAQEQKDSAEFDNVIAQVQATFTEALDHAIAVADSQFATQDEV
DAAWKALMNEIHKLGFVKGDISSLETLVQAAEDIDLTLYVEKGQAEFTAALQAAQAVVAD
KDNAMEQEIQEATDRLLDAMLELRVKADKSILQALLADAANVDVSLYTAETVATFQAAND
AAKDIYDNPDATQAEVNDAAQALQDAISGLKSADTSAQGAAVQGDANATTGSGNAKTGET
VPVAAAAALLLAGAAAIVFKKRLK

Enzyme Prediction     

No EC number prediction in MGYG000001332_01161.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	877	1403	1.2e-100	0.996031746031746
CBM67	680	855	1e-29	0.9602272727272727
CBM66	505	641	1.1e-19	0.9096774193548387
CBM66	172	292	8.5e-17	0.8064516129032258

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17389	Bac_rhamnosid6H	2.23e-31	989	1339	4	339	Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
pfam08531	Bac_rhamnosid_N	9.91e-24	703	848	1	153	Alpha-L-rhamnosidase N-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. This domain is probably involved in substrate recognition.
pfam05592	Bac_rhamnosid	7.62e-09	878	980	2	102	Bacterial alpha-L-rhamnosidase concanavalin-like domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
pfam17390	Bac_rhamnosid_C	1.94e-06	1342	1416	1	76	Bacterial alpha-L-rhamnosidase C-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
pfam07554	FIVAR	3.63e-06	1592	1650	3	68	FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SCF06921.1	4.12e-224	676	1439	158	925
ASO20813.1	7.30e-224	669	1440	138	918
AVT31771.1	2.60e-222	690	1439	164	921
AVT37928.1	2.60e-222	690	1439	164	921
APU21677.1	1.65e-218	669	1440	139	919

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W5M_A	7.19e-35	672	1439	288	1028	CrystalStructure of Streptomyces avermitilis alpha-L-rhamnosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3W5N_A Crystal Structure of Streptomyces avermitilis alpha-L-rhamnosidase complexed with L-rhamnose [Streptomyces avermitilis MA-4680 = NBRC 14893]
6I60_A	5.09e-31	707	1442	191	942	Structureof alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12],6I60_B Structure of alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12]
6GSZ_A	5.52e-28	706	1413	145	855	Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]
2OKX_A	1.70e-09	936	1408	485	947	Crystalstructure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1],2OKX_B Crystal structure of GH78 family rhamnosidase of Bacillus SP. GL1 AT 1.9 A [Bacillus sp. GL1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q82PP4	3.85e-34	672	1439	288	1028	Alpha-L-rhamnosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=SAVERM_828 PE=1 SV=1
T2KM26	6.17e-34	881	1423	604	1155	Bifunctional sulfatase/alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22250 PE=1 SV=2
T2KPL4	2.38e-11	45	157	35	156	Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22170 PE=2 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
0.000375	0.998795	0.000205	0.000254	0.000183	0.000157

TMHMM  Annotations     

start	end
1680	1699