CAZyme Information: MGYG000003012_02805

Basic Information

• Species: Blautia_A sp900540785
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp900540785
• CAZyme ID: MGYG000003012_02805
• CAZy Family: GH127
• CAZyme Description: Non-reducing end beta-L-arabinofuranosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
649	MGYG000003012_36|CGC2	74431.78	4.8293

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003012	3168635	MAG	United States	North America

• Gene Location: Start: 31034; End: 32983 Strand: -

Full Sequence      

MKGKLNSLPLGNIEIQDLFWNKYTELVRQVIIPYQWGILNDEIEGVETSHCIANFKIAAG
ESSGEFKGAVFQDTDVAKWLEAVGYSLSVHRDEDLEKIADETIDLIGRAQCEDGYLNTYF
TIKAPELRWTNLKEGHELYTAGHMIEAAVAYYQATGKKKFIEIVSKFADLIVQTFGSEDG
KIHGYPGHQEIELALVKLYRITKKKEYLETAKYFIDVRGENPNYFEEEEKKPLYQQIFPE
FSGYDLKYSQCHLPVRSQETAEGHAVRAVYMYCAMADLAYEYEDSELLEACDRLWENLTK
KRMYLTGSIGSSGLLERFTTDYDLPNDSNYSETCASIGLALFAKRMTEIKKDASYMDIAE
LALYNTVLSGIAMDGKSFFYVNPLEVWPDNCLERTSKEHVKPVRQKWFGVACCPPNIART
LASLGQYIYMKEGNTLYTNLYLSNKAEVDLENGRVEVKTETKFPFDGMIKMKAESTAQNW
KLALRIPEYVKKYQVYMNGAEVSNLNVEKGYLMLESSEGITEFSIKFELPVRFIRANPNV
RADAGKVAVMKGPLVYCLEETDNGQNLSEIFVDTVQTPKEEYREDLFKGCCVIRLKGKRL
KEENWKEGKLYQECEAFYEDTELTAIPYCYWCNRTPGEMAVWLKEAIHI

Enzyme Prediction     

No EC number prediction in MGYG000003012_02805.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH127	14	557	1.1e-215	0.9961832061068703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3533	COG3533	0.0	13	645	12	587	Uncharacterized conserved protein, DUF1680 family [Function unknown].
pfam07944	Glyco_hydro_127	4.60e-153	12	557	1	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	7.11e-05	85	212	553	677	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.
cd04434	LanC_like	0.004	147	335	108	295	Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWY98667.1	4.28e-315	2	648	3	657
QBE96220.1	2.13e-313	4	647	5	650
QMW80468.1	2.13e-313	4	647	5	650
QIB56758.1	2.13e-313	4	647	5	650
QAA32625.1	1.58e-311	4	647	8	651

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4QJY_A	2.39e-230	12	645	15	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	9.54e-225	12	645	15	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]
3WKW_A	6.67e-163	12	646	2	659	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	1.88e-162	12	646	2	659	ChainA, Non-reducing end beta-L-arabinofuranosidase [Bifidobacterium longum subsp. longum JCM 1217]
3WRE_A	1.89e-162	12	645	2	658	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
E8MGH8	1.03e-161	12	645	2	658	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
1.000044	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003012_02805.