CAZyme Information: MGYG000002359_00691

Basic Information

• Species: Mycobacterium tuberculosis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis
• CAZyme ID: MGYG000002359_00691
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1243		133410.23	6.0589

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002359	4387829	Isolate	Sweden	Europe

• Gene Location: Start: 744242; End: 747973 Strand: +

Full Sequence      

MDYLKPYWDTHPQDRADLRRFLADGRIEVMGGTYNEPNTNLTSPETTIRNLVHGIGFQRD
VLGAEPATAWQLDVFGHDPQFPGLAADAGLTSSSWARGPHHQWGPAQGGVDRMQFCSEFE
WIAPSGRGLLTHYMPAHYSAGWSMDSSTSLADAEAATYALFDQLKKVALTRNVLLPVGTD
YTPPNKWVTAIHRDWGARYTWPRFVCALPKEFFAAVRAELAKRGWVPSPQTRDMNPIYTG
KDVSYIDTKQANRAAENAVLEAERFAVFAALLTGAEYPQAALAKAWVQLAYGAHHDAITG
SESDQVYLDLLTGWRDAWELGRAARDNSLRLLSGAVAASHDRVVVWNPLTQRRTDIVTAR
VDPPLQAGVRVFDPDGAEVAALVEHDGRSVTWLACDVPSLGWRVYRLVPADEAPGWELVP
GTDIANEHYRLAVDPERGGALSSLVQDGRQLIAAGRVANELALYEEYPSHPTQGEGPWHL
LPTGPVVCSSACPAQVQAYRGPLGQRLVVRGRIGTLLRYTQTLTLWDGVDRVDCRTSIDE
FTGEDRLLRLRWPCPVPGAMPISEVGDAVVGRGFALLHEGPESVDTAQHPWTLDNPAYGW
FGLSSAVRVRAGDGVRAVSVAEVVSPTETVSGPMARDLMVALVRAGVTATCSGADKPRYG
HLDVDSNLPDARIALGGPDRNTFTKAVLAEAAPAYTAELQRQLAKTGTARVWVPAANPLA
RAWLPGADLRAPCALPVLVIDGRDEKHLRAAVASLADDLADAEIVVHQRAAPQMEPFEDR
TVALLNRGVPSFAVDSEGTLHTALMRSCTGWPSGVWIDQPRRTAPDGSNFQLQHWTHHFD
YALVCGGGDWRRAGIPARSAQFSHPLLAVAPRRPQGELPAVGSLLHVEPADSVQLGALKA
AGNPLAAGSARPVQPAAVALRLVQTTGADTPVTIGCELGKVGALRPADLLETPLAMARAR
KSSIDLHGYQVATVLARLDVAADMANVLAADDVALAPHAETAQPQYARYWLHNRGPAPLG
GLPAVAHLHPRRVRGQPGDDVVLRLTAASDCTDSVLGGVVDVVCPLGWPATPARLPFTLG
AGAHLQADIALSIPAGAPPGPYPVRAQLRVVDTAVPAAWRQVVEDVCVVTVGADSDLEEL
VYLVDGPADIELAAGDRARLAVTIGSRAHAELALDAHSISPWGTWEWIGPPALGAVLPAR
GMAKLAFDVTPPAWLEPGQWWALVRVGCAGQLVYSPAVKVSVT

Enzyme Prediction     

No EC number prediction in MGYG000002359_00691.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	2	238	1.3e-64	0.8029739776951673

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0383	AMS1	0.0	90	1242	9	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10786	GH38N_AMII_like	2.49e-73	1	205	50	251	N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). Alpha-mannosidases (EC 3.2.1.24) are extensively found in eukaryotes and play important roles in the processing of newly formed N-glycans and in degradation of mature glycoproteins. A deficiency of this enzyme causes the lysosomal storage disease alpha-mannosidosis. Many bacterial and archaeal species also possess putative alpha-mannosidases, but their activity and specificity is largely unknown. Based on different functional characteristics and sequence homology, alpha-mannosidases have been organized into two classes (class I, belonging to glycoside hydrolase family 47, and class II, belonging to glycoside hydrolase family 38). Members of this family corresponds to class II alpha-mannosidases (alphaMII), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst.
pfam01074	Glyco_hydro_38	5.69e-57	1	238	49	270	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
PRK09819	PRK09819	6.20e-20	2	558	60	627	mannosylglycerate hydrolase.
smart00872	Alpha-mann_mid	1.78e-19	237	314	5	79	Alpha mannosidase, middle domain. Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AMC44968.1	0.0	1	1243	1	1243
AGQ37073.1	0.0	1	1243	1	1243
BAQ04543.1	0.0	1	1243	1	1243
AID03722.1	0.0	1	1243	156	1398
AEB02792.1	0.0	1	1243	156	1398

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WYH_A	2.88e-12	2	336	82	414	Structureof the Streptococcus pyogenes family GH38 alpha-mannosidase [Streptococcus pyogenes M1 GAS],2WYH_B Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase [Streptococcus pyogenes M1 GAS],2WYI_A Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase complexed with swainsonine [Streptococcus pyogenes M1 GAS],2WYI_B Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase complexed with swainsonine [Streptococcus pyogenes M1 GAS]
5KBP_A	1.28e-10	4	403	61	482	Thecrystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],5KBP_B The crystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583]
6LZ1_A	1.61e-07	9	311	338	631	Structureof S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_B Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_C Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_D Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-]
7DD9_A	1.72e-07	9	311	338	631	ChainA, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_C Chain C, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_E Chain E, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_G Chain G, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54746	3.19e-17	4	555	59	624	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q91W89	3.71e-13	11	468	309	732	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
Q9NTJ4	2.48e-12	11	468	310	733	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
P21139	2.86e-11	9	604	307	859	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
Q16706	3.91e-07	1	408	216	721	Alpha-mannosidase 2 OS=Homo sapiens OX=9606 GN=MAN2A1 PE=1 SV=2

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
1.000043	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002359_00691.