dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000004085_00144

You are here: Home > Sequence: MGYG000004085_00144

Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UMGS1253; UMGS1253;

CAZyme ID

MGYG000004085_00144

CAZy Family

PL21

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1370		151861.09	4.3412

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004085	2144710	MAG	United Kingdom	Europe

Gene Location

Start: 154058; End: 158170 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000004085_00144.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
PL21	740	803	1.3e-21	0.9305555555555556
CBM32	1253	1365	1.9e-20	0.8870967741935484

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam07833	Cu_amine_oxidN1	1.22e-39	1137	1229	1	93	Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam00754	F5_F8_type_C	1.12e-16	1251	1365	5	127	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam07833	Cu_amine_oxidN1	2.02e-11	1119	1166	38	92	Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam18675	HepII_C	6.41e-11	1014	1097	1	86	Heparinase II C-terminal domain. Heparinase II (HepII) is an 85-kDa dimeric enzyme that depolymerizes both heparin and heparan sulfate glycosaminoglycans. The protein is composed of three domains: an N-terminal alpha-helical domain, a central two-layered beta-sheet domain, and a C-terminal domain forming a two-layered beta-sheet. The C-terminal domain contains nine beta-strands packed together in a manner resembling a beta-barrel.
pfam07833	Cu_amine_oxidN1	9.38e-10	1200	1230	2	32	Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI63941.1	3.10e-201	367	1097	32	789
BCI63940.1	1.60e-191	372	1094	41	788
BBH20141.1	1.11e-190	367	1361	228	1210
QDG70382.1	3.09e-155	206	1114	54	975
AYM77060.1	4.04e-153	222	1106	52	947

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2FUQ_A	2.35e-141	374	1095	19	743	ChainA, heparinase II protein [Pedobacter heparinus],2FUQ_B Chain B, heparinase II protein [Pedobacter heparinus]
3E80_A	2.49e-141	374	1095	21	745	Structureof Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus],3E80_B Structure of Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus],3E80_C Structure of Heparinase II complexed with heparan sulfate degradation disaccharide product [Pedobacter heparinus]
3E7J_A	1.35e-138	374	1095	21	745	ChainA, Heparinase II protein [Pedobacter heparinus],3E7J_B Chain B, Heparinase II protein [Pedobacter heparinus]
2FUT_A	2.66e-135	374	1095	20	744	ChainA, heparinase II protein [Pedobacter heparinus],2FUT_B Chain B, heparinase II protein [Pedobacter heparinus]
5ZU6_A	3.16e-11	1246	1362	35	151	ACBM32 derived from alginate lyase B (AlyB-OU02) [Vibrio]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C6XZB6	2.63e-140	374	1095	44	768	Heparin and heparin-sulfate lyase OS=Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3) OX=485917 GN=hepB PE=1 SV=1
P46883	5.81e-06	1133	1219	26	114	Primary amine oxidase OS=Escherichia coli (strain K12) OX=83333 GN=tynA PE=1 SV=1
P80695	7.61e-06	1142	1219	34	111	Primary amine oxidase OS=Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686 / BUCSAV 143 / CCM 1901) OX=1006551 GN=maoA PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.005131	0.970067	0.023167	0.000889	0.000388	0.000324

TMHMM Annotations download full data without filtering help

start	end
7	29