CAZyme Information: MGYG000004133_00804

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; HGM11514; HGM11514
• CAZyme ID: MGYG000004133_00804
• CAZy Family: GH141
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
830		91564.47	4.4563

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004133	2160156	MAG	United Kingdom	Europe

• Gene Location: Start: 56691; End: 59183 Strand: -

Full Sequence      

MKATKKILAIMLVLAIAVSVFASFGAVSASGGEIYVSTTGSDSADGTRENPVATLKKACE
LAGEGATIIISDGTYTVSDSAEITKNNITVKAQPGANVVLTGATQLDATKFKKVTDTEIL
DRIIDKTAKEKVVAVNLNDLGVTEFGTINMSGFAYGDTPMNPQLIVNGKRQVLARYPDKD
YLYISKVIESGPNLREKPAGATIADYKGQGMKFQVSDSRLSKWTKAEDLWVFGYFMYDWA
EANLSAKIDFENSNTVSTEYPSYFCVTEDRRLYFYNLLEELSVPGEWYIDRNSGILYIYP
EQTMKASDVVEFITYAKPFICVNGAENVKIQGIKFEKSLDMGVKINDSKNVTVSECTFNE
ISYTAVNSLTSYETKVDRCAFTEVGYRAVYIESGDVAKLIPGGSEITNCTVKGFARIKPT
SAPAFWIRGVGNKVAHNEINDGPYIAIWFGGNDNIIEYNEISEVCKDTADVGAIYAGREW
SSRGNEVRYNYIHDIKIINTTTGMKVQAIYLDDQFSSANVHGNIIKNVPSVALYGGGRYN
TFVNNIVLEAQEPFVFDERGIKEGQCGEGSEIRTKLKALPYDTGIWKEKYPELANILNDE
PELPKYNVIKGNLSYNIPNYDIVNDVKLYGEFQEDVAVKPSDFVDYKGGDLTLKDDSEVF
TKLPDFEKIDFKAIGVEEKAPEKTADSVLENSVALMINKLETYVFGSKSPIDVPPMIVND
RTVVPVRFIAESFGADVSWDDATKKVTVKKDDSTIELYIDKAEISVDGETSTLDTAAQII
DGRTMLPLRAVVEALGKEVFWDARGLIVISDSEIVTDEDAQAVSDIVSKF

Enzyme Prediction     

No EC number prediction in MGYG000004133_00804.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH141	33	336	1.5e-26	0.5256166982922201

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam07833	Cu_amine_oxidN1	1.39e-32	718	809	1	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.
pfam07833	Cu_amine_oxidN1	1.36e-14	690	748	35	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.
pfam13229	Beta_helix	1.06e-11	342	545	2	156	Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.
cd14251	PL-6	0.001	53	106	5	62	Polysaccharide Lyase Family 6. Polysaccharide Lyase Family 6 is a family of beta-helical polysaccharide lyases. Members include alginate lyase (EC 4.2.2.3) and chondroitinase B (EC 4.2.2.19). Chondroitinase B is an enzyme that only cleaves the beta-(1,4)-linkage of dermatan sulfate (DS), leading to 4,5-unsaturated dermatan sulfate disaccharides as the product. DS is a highly sulfated, unbranched polysaccharide belonging to a family of glycosaminoglycans (GAGs) composed of alternating hexosamine (gluco- or galactosamine) and uronic acid (D-glucuronic or L-iduronic acid) moieties. DS contains alternating 1,4-beta-D-galactosamine (GalNac) and 1,3-alpha-L-iduronic acid units. The related chondroitin sulfate (CS) contains alternating GalNac and 1,3-beta-D-glucuronic acid units. Alginate lyases (known as either mannuronate (EC 4.2.2.3) or guluronate lyases (EC 4.2.2.11) catalyze the degradation of alginate, a copolymer of alpha-L-guluronate and its C5 epimer beta-D-mannuronate.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUH28384.1	3.78e-117	35	677	41	727
QNK56945.1	7.66e-66	28	676	34	731
AUP78440.1	5.13e-65	33	553	26	579
QUT84604.1	1.07e-48	144	677	160	721
AWN48906.1	2.98e-43	198	613	176	587

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5MQP_A	4.39e-08	30	337	23	321	Glycosidehydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_B Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_C Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_D Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_E Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_F Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_G Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron],5MQP_H Glycoside hydrolase BT_1002 [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000359	0.998954	0.000169	0.000192	0.000170	0.000154

TMHMM  Annotations     

start	end
7	29