CAZyme Information: MGYG000003436_01980

Basic Information

• Species: HGM20899 sp900767005
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Succinivibrionaceae; HGM20899; HGM20899 sp900767005
• CAZyme ID: MGYG000003436_01980
• CAZy Family: CBM74
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1824		196065.3	4.5456

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003436	2378747	MAG	Fiji	Oceania

• Gene Location: Start: 5403; End: 10877 Strand: -

Full Sequence      

MKLNKLALFVASAMAVTACGGGSGSSDNGSNPAPQATTVSQSVTVDRYSDPNVEAQAQQV
LGDTASAQVASEDEQTLVCLDTNNNGSCSDETTTKVLDSGVGSTTLEWSSNIDTSNLNIV
AQNKKFVYKVKASEGGNAQTRTPLFVNPLTDAATRLGKEKFAQAVGYTGDVNTFSATKDY
SGLDESVQVLSDSVASIAASDTTGVYDEETVLDKLGSIFTKIVDQLQNAKISKVQIVINI
ILNQDVDPADPDKKNNVPVASFEYIVGQNGVVTFTNKSTDADGDKLVYNWTFGDGASSKD
VAPTHTYNTNNTYKVTLVVSDGKDTDVLRKEVTVDTVTIEKPFEPAFNYTTDGLTVKITN
TTKDVDDNTQYRWDFGDGSELSTEKNPTHSYAQNGTYTIKMQAMSSTGAKKVVTKENVKV
SGGEGPIDVVTLSVSDISASTNNLSASFVANVNYNGKASISYVWNFGDGKTLETSSNKAT
HTYANEGTYSVSVVAKDANGVTGSKSISGVNVKKNVVPPVDVCPTDNPFCKGDIDPAECV
QTCEEKEIEVCPETATAQTAADSSSLTAIETQYYKTNPNGQVGKNKTITGPSDWTTDMIV
AQGAANDDPRAYRGYHEKATDFYAMYAAWDDTNLYLMVEMPNIEGKENGGDFDYSNDQFL
PMGIGIRTGKRPAGNGLMVDGNNVWTAGKFYTIEEGIDTLLMFHPRLPTVNKPGLFKTNS
EGLFSYETEDGSLLGFDEAKIERVNTPGTKSANYWGISDNYGGAKDNYLTGSYEDLLAKN
ANASGHLYQITIPLASIDITKDYLETNGIAVVAFSTFGESMMDALPWTPNLVDVASEAYS
KDDSTSQEKEDFDLYDVPLARVGKFNGVIPTPTPTPTPTPCTTKKITVCTPETLPATCQS
SGSIDVKLSHSEQESADKVTTNVNVATGYKGVTYTWEVTGSKAVTSSYDKTSKSFSIPKK
NKAQNVTVKVTAKNASGTKIGSESFSFDVPACEDCGINPPVDSWVENQGIDSDNIKIYDP
NNTCKAQDGAIVLKADAESAPNLYAYGNDASEVALTAKWPGDSLTKIDGCTSTFYQSKAN
LLPNSGAKAIFNGVNGDRYPADMQPGVEMTAAKACFDWESKKALPLEECGLGASAPKDTA
YILKNGSEVQDGSTIVISYNEEVPTTAYVDVSLMVYGEKTDASTLGTYTINDKSGQFTNG
QIIRVGQNIPAAEDKASAEPMVLTVSYGDVTKTFKFIKVKYQKPQAVTQFSWNNALMYFV
MTDRFYNGDKSNDNSYGRPYKDATGHATATFHGGDIKGMTERLDYIKSLGMNAIWITAPY
EQSHGWTGGGSSGAFAHYAYHGYYALDFTSLDKNVGTVDEFRTFVTEAHKRGIRVVLDIV
MNHSGYATLQDMCDYGFGVRSDGKSACDPWQPGSGETWHNKPISEESNAAWNGWWGKDWI
KFGGYGEQCGAGDGLDACVSFLPDFKNSQTHGSSVSVPKFLQTKWSKADAEHDIPAAKAY
RSGNMSVAEFEAHWLASWVEEFGIDGFRCDTAKHVTKSTWKLLKDLSNEALAKWRANNAG
DDPAASWTDKFWMTGEHWGYKTDPTDGGAYASQGGFDSMINFSFNGQSNGSCSAPTVSSW
DSYASMYGVGSGSPKLNALTYISSHDTSLCRPGNMKDLGTAFLLLPGGVQVYYGDETARK
NDNGGSGNDPEHGTRSDMNFPSDISSQATWAANVDTLSTSFSSDATLAHWQKIGQFRYRN
AAVGAGKQTKTSDGSYCRTYNDEESGINNSVVIHVGSASSVDVGSCFADGTELQDAYSGK
TATVSGGKVTLSGAGDLILLELKR

Enzyme Prediction     

EC	3.2.1.98	3.2.1.60	3.2.1.-	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1294	1677	5.6e-123	0.9972222222222222
CBM74	574	861	7.6e-57	0.9967948717948718

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	1.19e-178	1238	1756	176	663	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	3.95e-49	1257	1737	5	341	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.
COG0366	AmyA	1.25e-41	1255	1750	1	446	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.04e-39	1257	1673	2	253	Alpha amylase catalytic domain family. 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; and 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 this 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.
cd11340	AmyAc_bac_CMD_like_3	8.31e-39	1257	1732	6	406	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKH59997.1	7.08e-148	1250	1820	44	592
AZK49196.1	9.30e-148	1250	1821	129	672
CQR56565.1	1.27e-146	1245	1821	55	608
CAK97857.1	1.48e-146	1250	1821	7	552
ALA51229.1	3.65e-144	1242	1820	24	575

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	5.73e-28	1248	1703	2	347	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	9.87e-28	1248	1703	36	381	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
6SAO_A	1.34e-23	1252	1812	6	426	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
4E2O_A	6.80e-23	1251	1541	6	202	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1JF5_A	2.71e-19	1255	1551	131	350	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF5_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	1.22e-114	1250	1749	184	649	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P21543	2.21e-23	1252	1550	744	958	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q05884	9.37e-19	1291	1817	95	616	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
Q58863	2.28e-18	255	524	721	987	Uncharacterized protein MJ1468 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1468 PE=4 SV=1
Q08751	3.43e-18	1255	1551	131	350	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000035	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003436_01980.