CAZyme Information: MGYG000001265_01624

Basic Information

• Species: Methylobacterium sp002778835
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Beijerinckiaceae; Methylobacterium; Methylobacterium sp002778835
• CAZyme ID: MGYG000001265_01624
• CAZy Family: GH77
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1630		178653.26	5.2104

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001265	4213059	MAG	Italy	Europe

• Gene Location: Start: 4499; End: 9391 Strand: -

Full Sequence      

MSGALQRLADLVGVASGYTDAFGQGVETSLETRKGMLRALGFAVGSEEEIAASLAEVQAL
RQGLIPPLIAVEARRASEVPVRAEGGTAAWRIEDEREGVREGREAVSAEGILELPPLTPG
YHRITVTVGERSASGWIVAAPQRCWRPRAYAEEGSNDWGLAAQLYGLRSPHNLGIGSYTD
AGRAARDAGLRGASFLGLSPVHALFESDRTKISPYSPSSRLFLETLFIEPGALPGFAGSR
AEAMLAKARTRVDALRDAALVDHAGIWEVLSPVLRAYWEDSDARSGADAAFDAFREAGGE
DLRSHATFEALSAHFKAEGAHWLGDWPEEYRRAGTQAVSAFAEEHAEEVAYHAFLQFLAD
RQLAQAAEAALDSGMRLGLYRDLAVGADRGGSEVWSHPERFAGHVSIGAPPDLLAPKGQD
WGLPAFDPLAMERDGLAAFRALVQANMRHAGAIRIDHAFQLARLFLIPTDGTAHDGAYVA
MPFEAMLAVLRLESHRHQCLVIAEDLGTAPQGFSDALMAAGILSYRILAFERLGDGRFKA
PEDYPRDALTAITTHDLPTFVGWWRGVDTDTRQSLGLYDADRAEAERRERVTERARLTEA
LASQQLLPGYDPPEAAPFEAATRYLARAPSMLTAVQYEDVVSELSQANVPGSTEGYPNWR
RKLDRTLDSIAAPGGPLAKLAAALAAEERGPRSGAARLAVPPPRATYRLQFHKDFTFADA
ARIAPYLARLGISHVYASPLQKARPGSTHGYDIVDHSAINPELGGEEGFIALSEALKENG
LKLLLDIVPNHMGVGGSDNPWWLSVLEWGPLSPFAHAFDIDWERLGANRNLVIPFLGDRY
GEALEKGDLELKFDAASGAFSVWHYDHQFPIRPLDYPTVLDRVLAAMVEVDEDAAGGLLG
VAERLRAMGEETNAERRQTFPAEAEGLKQRLADLYGASPAIREAMARTLRLLNGRKGHPE
SFGPLHRLLESQAYRLAHWRVAASDINYRRFFDVNSLAGLRVEKSDIFHRAHETVFRHVR
EGRIDGLRIDHIDGLADPQGYARALQAAVGPGFYVVVEKILEPGERLRPWPVAGTTGYDV
LNQLDGILVDRGKQARIERLYGWATDADEEYGFQLRAAKAEILEISFASELEVLTNDLKQ
IADADRRTRDFSVNAIRRALIEIIARFPTYRSYLPSDLDESDVEPEDVRLIEGAVAKAKR
WSALPDRSVHDFAAAALLGEVDTDGPARPDPRLVLRFRRRFQQLTGPVMAKSLEDTLFYR
YVLLLGLNEVGGDPGEYGITVEHFHALQAARARDWPNAMIATATHDTKRGEDARTRQLAL
SEMPEEWARAWDAWRETAGPHLTRVEGEPAPDANDQWMFLQAILGAWPLELIDEDVPAEV
ESFRDRLIAYSEKALREGKRHSNWVNIDEAYEGAVRNLFAAIIAPGSAFLARLRPLARRL
ACLGMIAGLGRTVLKATLPGVPDTYQGTEFWDFSFVDPDNRRPVDYGARAEALTIEVPAA
DLLASWRDGRVKQAVLSRLLADRAADPRFYADAGYEPVIATGTRAQNLVAFRRVGETSGA
NDLLVAVPRLVANLVGTEPWSGSAFSGTVLTLSDPGRWHDLVTGAEHTGASLDAGELFAS
LPFAVLRRAG

Enzyme Prediction     

No EC number prediction in MGYG000001265_01624.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH77	163	671	1.7e-140	0.9595141700404858
GH13	724	1086	4.3e-121	0.9898648648648649

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11336	AmyAc_MTSase	0.0	705	1525	1	659	Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase). Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
COG3280	TreY	0.0	703	1629	4	889	Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism].
PRK11052	malQ	0.0	1	672	2	674	4-alpha-glucanotransferase; Provisional
PRK14507	PRK14507	0.0	1	1630	4	1692	malto-oligosyltrehalose synthase.
PRK14511	PRK14511	0.0	699	1630	1	879	malto-oligosyltrehalose synthase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWN38642.1	0.0	1	1628	1	1630
ACB23595.1	0.0	4	1628	3	1631
QGY05843.1	0.0	5	1628	4	1635
AYO81978.1	0.0	5	1629	4	1638
AWV18001.1	0.0	5	1628	4	1631

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LCV_A	2.42e-130	703	1626	2	754	structureof Mutant S44P of maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
6LCU_A	3.20e-129	703	1626	2	754	structureof maltooligosyltrehalose synthase from Arthrobacter ramosus [Arthrobacter ramosus]
4S3P_A	1.47e-107	5	675	6	675	AmylomaltaseMalQ from Escherichia coli, apo structure [Escherichia coli K-12],4S3P_B Amylomaltase MalQ from Escherichia coli, apo structure [Escherichia coli K-12],4S3Q_A Amylomaltase MalQ from Escherichia coli in complex with maltose [Escherichia coli K-12],4S3Q_B Amylomaltase MalQ from Escherichia coli in complex with maltose [Escherichia coli K-12],4S3Q_C Amylomaltase MalQ from Escherichia coli in complex with maltose [Escherichia coli K-12]
4S3R_A	4.50e-103	5	675	6	675	AmylomaltaseMalQ from Escherichia coli in complex with the pseudo-heptasaccharide acarviosine-glucose-acarbose [Escherichia coli K-12]
5ZCR_A	2.12e-90	706	1538	5	664	DSM5389glycosyltrehalose synthase [Saccharolobus shibatae B12],5ZCR_B DSM5389 glycosyltrehalose synthase [Saccharolobus shibatae B12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q44315	3.15e-142	703	1626	4	767	Maltooligosyl trehalose synthase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treY PE=1 SV=1
P9WQ20	1.10e-128	702	1628	4	762	Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treY PE=3 SV=1
P9WQ21	1.10e-128	702	1628	4	762	Putative maltooligosyl trehalose synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treY PE=1 SV=1
P15977	7.65e-107	5	675	6	675	4-alpha-glucanotransferase OS=Escherichia coli (strain K12) OX=83333 GN=malQ PE=1 SV=2
P45176	4.11e-86	111	670	104	680	4-alpha-glucanotransferase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=malQ PE=3 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
1.000054	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001265_01624.