CAZyme Information: MGYG000004085_00823

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UMGS1253; UMGS1253
• CAZyme ID: MGYG000004085_00823
• CAZy Family: PL35
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1410		154834.24	4.3994

Genome Property

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

• Gene Location: Start: 20412; End: 24644 Strand: -

Full Sequence      

MMRSKAIIWALVMALVVTCFPTLSFAADDVGEAIFYNRTYDEEGKALEDGLIVMPKSNSI
ALEKEGDNQYVKIQMADAVTEDCYIEVSMPNPTKYIVVEMDLSSTKAGISGDLQFKDSSR
TDGRLFKISNGKIISAGSEKELGTLKKGKWLNVAAVLNLETFTYDSYVDGKQVEKGVPVS
GAATGLTLLRLYIAKSGNGADLLVDNLKIYEATEPKDITGKDVQEPTNTFTPSAAPSSTP
DSNVTMKGKTAVFDCDDKDAIKAMGLTADSKNVKSAKYSAEWKFADKPNLIFNSISGDLR
CYTEYSFNIYNSSDKEQKLYMRFDSQNAATTDGDDYYGRSLTLAPQAWTEVKGTFASLGK
TRTPIGWHQIDSLKLFSTGWGMENDTSTVLYLDTIYLDGSNVEATPVPTANPSDFSRVEN
AVCLKLDCPSALVKKEKLPIDENNANVVPFTSNDRTLVPMRFISEAFGAEVSYDGGATEK
VTVKLGNDTIELTIGSDKIYKNGQEIQIDTAAIVTGDDRTFVPLRAIAEALGKQVFWDDM
GLIVISDTENIFNRDTDLALMLNVMAEFTYERPGGEKIISDLKANAPQHPRILANADDFA
RIKSLYDTDPLMKEWIDKQLKNAENTAASAQPPVYSVDEGGRLKGTNTESYMLQWGLAYQ
MTGDQKYVDAAYDHIEVLCGFDNWHPGHFLDAAGIMKGVAIGYDWMYDGFTDEQRKVIEK
GLFEHGIQAGIGAYAGTTEDMEPKHGTFGRSGWTNTDNNWNAVCNGGLTLACAAIGDLPE
YEKDAGDLMGKVLKSIEKGIRCYAPDGSYPEGPGYWAYGTNNLFYMIECLDSAMGTDYGL
FNAPGLDTTCYFPNYIEGTNGMWNFNDCGEGTVDTSHLFWVANKIGNPDLAGMRLQDITS
GRKAAGIHDILHYDLNNINKEVHLPLDRYMTGVETVTMRGDWNDSGTVFTGLHGGYNGVN
HGNLDSGNFVIDAGGVRFISDIGTENYNLPSYFSGGAGGTRWTYYRNRAEGHNTITVNPG
TSEDQVVSATTKITRHESKPRGAIAVVDMAPAHGNKVKEAQRGILFTDNRKAVVVQDEMT
LPSASEVWWFAHVQDGEITVAPDGKSAVIEKAGKRMWVGIVSDMADAKFEVMAADPLPTS
PQKNEAEYDRSAWKKLAIHMSGVTDYKLAVEFRLLEGTQTEPDYKYTYTDIADWTIPDGE
IVIPRLTDLTVDGQTVGNFSPLATNYEVVLPYGTTAVPTVNATAEDGYTVEITQAAALPG
IASVRVYDPNDPETYNIYDITLRAMAEIEVEASDVPEPANVPANTLDGDLGTRWAAEGEQ
WIKYTFANPREISSVWIAFWKSNERSTMFKLEISEDGENFETVFDGTQTNKEDTLAEYKL
PQPTTVKAVRISGSGNTSNAWNSILEVEFK

Enzyme Prediction     

No EC number prediction in MGYG000004085_00823.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL35	947	1123	1e-48	0.9720670391061452
CBM32	1292	1407	1.3e-20	0.9112903225806451

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam07833	Cu_amine_oxidN1	1.75e-30	452	539	1	86	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	3.25e-16	1289	1407	1	127	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam07833	Cu_amine_oxidN1	4.34e-07	437	483	39	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.
pfam07940	Hepar_II_III	2.23e-04	947	1113	25	185	Heparinase II/III-like protein. This family features sequences that are similar to a region of the Flavobacterium heparinum proteins heparinase II and heparinase III. The former is known to degrade heparin and heparin sulphate, whereas the latter predominantly degrades heparin sulphate. Both are secreted into the periplasmic space upon induction with heparin.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALS27107.1	8.78e-169	570	1406	678	1507
AZS17848.1	1.99e-152	416	1407	275	1274
QNK56587.1	6.19e-152	588	1408	220	1024
QNK58643.1	9.79e-151	570	1408	773	1607
SDS98549.1	1.02e-148	587	1407	50	855

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7D29_A	1.82e-17	1300	1407	22	129	CBM32of AlyQ [Persicobacter sp. CCB-QB2],7D2A_A CBM32 of AlyQ in complex with 4,5-unsaturated mannuronic acid [Persicobacter sp. CCB-QB2]
2JD9_A	1.04e-16	1297	1407	21	131	Structureof a pectin binding carbohydrate binding module determined in an orthorhombic crystal form. [Yersinia enterocolitica],2JDA_A Structure of a pectin binding carbohydrate binding module determined in an monoclinic crystal form. [Yersinia enterocolitica],2JDA_B Structure of a pectin binding carbohydrate binding module determined in an monoclinic crystal form. [Yersinia enterocolitica]
5XNR_A	1.31e-15	1300	1407	22	129	TruncatedAlyQ with CBM32 and alginate lyase domains [Persicobacter sp. CCB-QB2]
5ZU6_A	7.05e-14	1290	1404	35	151	ACBM32 derived from alginate lyase B (AlyB-OU02) [Vibrio]
5ZU5_A	2.72e-12	1290	1404	35	151	Crystalstructure of a full length alginate lyase with CBM domain [Vibrio splendidus]

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
0.000677	0.609276	0.389291	0.000262	0.000246	0.000221

TMHMM  Annotations     

start	end
7	26