CAZyme Information: MGYG000001965_02518

Basic Information

• Species: CAG-510 sp900550475
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-510; CAG-510 sp900550475
• CAZyme ID: MGYG000001965_02518
• CAZy Family: GH127
• CAZyme Description: Non-reducing end beta-L-arabinofuranosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
641	MGYG000001965_39|CGC1	72930.69	5.5212

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001965	2761020	MAG	Denmark	Europe

• Gene Location: Start: 2543; End: 4468 Strand: +

Full Sequence      

MENGLWKFHIRDSFMGRYEKLIREEVIPYQEKALKDEIPGAEKSHCIENFRLAAEKLRTG
KCSGDFYGMVFQDSDVAKWLEGAAYSLVLFPDPELERRCDEIIGLIGEAQQPDGYLNTFF
TVKRPGQRWTCLWQAHELYCAGHLIEAAVAYDRCTGKKKLLEIMCRMADHIYTHFIEEGA
EGYPGHPEIELALMRLYHHTKNRKYLELAEHFINVRGVDPEYYAKEREKYGWDVWGGNPH
DTAYNQADKPVRQQDQATGHAVRAVYLYTGMADVARETGDEELLAACRRLWDNVVERRMY
VTGAIGSAYEGEAFTADYHLPNDTAYAETCASIGLIFFARQMLSAEKNSKYADVMERALY
NCVLAGMQLDGKRFFYVNPLESLPGISGVAVTHRHALPERPKWFTCACCPPNVARLLPSL
ANYAWDMEDGTVYHHLFIGGELDLREELGGTVMVETGYPYDGNVTYRFRPEAESMEMTLA
VRIPGFSRHTAIRKNGEEISCERKDGYAYLHGTFTENDTIVIELDMSVQTIYANSRISAD
SGKVAFQRGPLVYCAEQADNLEGVLPLAVRKNAAAEAKLHPTPRLHGIVKLELPGYRIQE
EQAPYSFDRPARETCEITLIPYYAWANRGKGEMRVWLPEAE

Enzyme Prediction     

EC	3.2.1.185

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH127	9	554	1.9e-214	0.9961832061068703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3533	COG3533	0.0	12	641	16	589	Uncharacterized conserved protein, DUF1680 family [Function unknown].
pfam07944	Glyco_hydro_127	2.03e-160	9	554	3	503	Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
cd04792	LanM-like	2.57e-05	82	230	550	687	Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.
pfam05147	LANC_like	0.001	72	241	72	216	Lanthionine synthetase C-like protein. Lanthionines are thioether bridges that are putatively generated by dehydration of Ser and Thr residues followed by addition of cysteine residues within the peptide. This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 (P40 seven-transmembrane-domain protein) and LANCL2 (testes-specific adriamycin sensitivity protein) are thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. Lanthionines are found in lantibiotics, which are peptide-derived, post-translationally modified antimicrobials produced by several bacterial strains. This region contains seven internal repeats.
cd04791	LanC_SerThrkinase	0.009	155	303	102	243	Lanthionine synthetase C-like domain associated with serine/threonine kinases. Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHQ60849.1	0.0	1	641	1	639
BCN30788.1	9.36e-315	1	641	1	640
QEH67728.1	1.66e-312	1	639	1	637
ADZ82012.1	1.35e-311	1	639	1	637
AEN95763.1	4.00e-235	2	639	14	645

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4QJY_A	1.47e-211	9	639	17	647	Crystalstructure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QJY_B Crystal structure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]
4QK0_A	4.89e-202	9	639	17	647	Crystalstructure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_B Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_C Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_D Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]
3WRE_A	8.08e-165	10	636	5	655	Thecrystal structure of native HypBA1 from Bifidobacterium longum JCM 1217 [Bifidobacterium longum subsp. longum JCM 1217],3WRG_A The complex structure of HypBA1 with L-arabinose [Bifidobacterium longum subsp. longum JCM 1217]
3WKW_A	1.14e-164	10	636	5	655	Crystalstructure of GH127 beta-L-arabinofuranosidase HypBA1 from Bifidobacterium longum ligand free form [Bifidobacterium longum subsp. longum JCM 1217],3WKX_A Crystal structure of GH127 beta-L-arabinofuranosidase HypBA1 from Bifidobacterium longum arabinose complex form [Bifidobacterium longum subsp. longum JCM 1217],7BZL_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7DIF_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7EXV_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217],7EXW_A Chain A, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217]
7EXU_A	3.22e-164	10	636	5	655	ChainA, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
E8MGH8	4.42e-164	10	636	5	655	Non-reducing end beta-L-arabinofuranosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001965_02518.