CAZyme Information: MGYG000001812_00523

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829
• CAZyme ID: MGYG000001812_00523
• CAZy Family: GH127
• CAZyme Description: Non-reducing end beta-L-arabinofuranosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
636	MGYG000001812_15|CGC1	71610.55	6.2165

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001812	3064175	MAG	Denmark	Europe

• Gene Location: Start: 5456; End: 7366 Strand: +

Full Sequence      

MMKCWESTVPGQVRLEDTFFKVWTEKNRLSTLPSALRKCRESGRIDAFRLNWKEGMANKP
HPYWDSDVAKVLECMAYELMTEPDRELEKELEEIVALIVSSQGKDGYLNSYYSVVEPEKR
WKDLAYGHELYCAGHLMEAAVAHFQATGRRNFLDCMCRCADYIASVFGRGEGRIRGYPGH
PEIELALCRLAKAADRKRYLELAKFFIDERGREPRYYACVEGIKNEANLKQLQAHRPLRE
QNEAVGHAVRAVYLYSGMADVAAATDDAELLELCRTLFRNIAERKMYITGGIGATREGEA
FLEEWNLPNAEAYAESCAAIGLVFFAERMLNITGDSCYADVMERVLYNGALSGIGLSGDV
FYYANPLEMNPGIRLPEPYSADRRPWFSCSCCPTNYCRFLPGIATRLWSVKEETEEKTGA
AAVRLNIPAASVYDDSRGRIRVSGAYPYDGRFEVLFESDFPGTFSFRIPEYCGGAFQSTL
NGRSVRLPVDGHGYALLEGMKKKGDCLEVNLNMPVRVMRSHPSLLQNHGRIALTRGPLVY
ALESADNPPGLERLLIPADQSFQTLPAASGSLPPGTLFIRGTAFREKERPADAPLYSSDS
PDFEKVPFTALPYALRQNRGGNEMILWVREKYSKDF

Enzyme Prediction     

No EC number prediction in MGYG000001812_00523.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH127	13	541	2.3e-175	0.9980916030534351

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3533	COG3533	2.50e-157	19	631	22	588	Uncharacterized conserved protein, DUF1680 family [Function unknown].
pfam07944	Glyco_hydro_127	2.34e-122	12	541	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.
cd06240	M14-like	5.50e-04	75	135	24	86	Peptidase M14-like domain; uncharacterized subgroup. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which 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. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM46834.1	1.10e-204	2	629	1	620
BBH85646.1	2.18e-163	13	630	15	629
AGT32221.1	7.12e-160	12	632	7	641
AGE22473.1	9.56e-157	63	631	69	643
QOR85903.1	1.05e-156	63	631	72	646

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4QJY_A	9.17e-157	9	631	12	648	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	5.17e-150	9	631	12	648	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]
6EX6_A	3.60e-113	13	628	15	623	TheGH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482],6EX6_B The GH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482]
3WRE_A	1.10e-96	63	629	73	657	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	1.45e-96	63	629	73	657	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
E8MGH8	6.04e-96	63	629	73	657	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
1.000047	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001812_00523.