Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF16657e5jy7A2 A: beta sandwichesX: Glycosyl hydrolase domain-likeH: Glycosyl hydrolase domain (From Topology)T: Glycosyl hydrolase domainF: PF16657ECOD (1.6)
APF00128e5jy7A1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00128ECOD (1.6)
BPF16657e5jy7B1 A: beta sandwichesX: Glycosyl hydrolase domain-likeH: Glycosyl hydrolase domain (From Topology)T: Glycosyl hydrolase domainF: PF16657ECOD (1.6)
BPF00128e5jy7B2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00128ECOD (1.6)
DPF16657e5jy7D2 A: beta sandwichesX: Glycosyl hydrolase domain-likeH: Glycosyl hydrolase domain (From Topology)T: Glycosyl hydrolase domainF: PF16657ECOD (1.6)
DPF00128e5jy7D1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00128ECOD (1.6)
EPF16657e5jy7E2 A: beta sandwichesX: Glycosyl hydrolase domain-likeH: Glycosyl hydrolase domain (From Topology)T: Glycosyl hydrolase domainF: PF16657ECOD (1.6)
EPF00128e5jy7E1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00128ECOD (1.6)
FPF16657e5jy7F1 A: beta sandwichesX: Glycosyl hydrolase domain-likeH: Glycosyl hydrolase domain (From Topology)T: Glycosyl hydrolase domainF: PF16657ECOD (1.6)
FPF00128e5jy7F2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00128ECOD (1.6)
GPF16657e5jy7G1 A: beta sandwichesX: Glycosyl hydrolase domain-likeH: Glycosyl hydrolase domain (From Topology)T: Glycosyl hydrolase domainF: PF16657ECOD (1.6)
GPF00128e5jy7G2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00128ECOD (1.6)
HPF16657e5jy7H2 A: beta sandwichesX: Glycosyl hydrolase domain-likeH: Glycosyl hydrolase domain (From Topology)T: Glycosyl hydrolase domainF: PF16657ECOD (1.6)
HPF00128e5jy7H1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00128ECOD (1.6)
CPF16657e5jy7C2 A: beta sandwichesX: Glycosyl hydrolase domain-likeH: Glycosyl hydrolase domain (From Topology)T: Glycosyl hydrolase domainF: PF16657ECOD (1.6)
CPF00128e5jy7C1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00128ECOD (1.6)
JPF18085e5jy7J1 A: a+b two layersX: Cystatin-likeH: Maltokinase N-terminal domain (From Topology)T: Maltokinase N-terminal domainF: PF18085ECOD (1.6)
JPF01636e5jy7J2 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: PF01636ECOD (1.6)
KPF01636e5jy7K1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: PF01636ECOD (1.6)
MPF18085e5jy7M1 A: a+b two layersX: Cystatin-likeH: Maltokinase N-terminal domain (From Topology)T: Maltokinase N-terminal domainF: PF18085ECOD (1.6)
MPF01636e5jy7M2 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: PF01636ECOD (1.6)
NF_UNCLASSIFIEDe5jy7N1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: F_UNCLASSIFIEDECOD (1.6)
IPF18085e5jy7I1 A: a+b two layersX: Cystatin-likeH: Maltokinase N-terminal domain (From Topology)T: Maltokinase N-terminal domainF: PF18085ECOD (1.6)
IPF01636e5jy7I2 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: PF01636ECOD (1.6)
LPF18085e5jy7L2 A: a+b two layersX: Cystatin-likeH: Maltokinase N-terminal domain (From Topology)T: Maltokinase N-terminal domainF: PF18085ECOD (1.6)
LPF01636e5jy7L1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: PF01636ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.20.20.80 Alpha Beta Alpha-Beta Barrel TIM Barrel GlycosidasesCATH (4.3.0)
A3.90.400.10 Alpha Beta Alpha-Beta Complex Oligo-1,6-glucosidase domain 2CATH (4.3.0)
A2.60.40.1180 Mainly Beta Sandwich Immunoglobulin-like Golgi alpha-mannosidase IICATH (4.3.0)
B3.20.20.80 Alpha Beta Alpha-Beta Barrel TIM Barrel GlycosidasesCATH (4.3.0)
B3.90.400.10 Alpha Beta Alpha-Beta Complex Oligo-1,6-glucosidase domain 2CATH (4.3.0)
B2.60.40.1180 Mainly Beta Sandwich Immunoglobulin-like Golgi alpha-mannosidase IICATH (4.3.0)
D3.20.20.80 Alpha Beta Alpha-Beta Barrel TIM Barrel GlycosidasesCATH (4.3.0)
D3.90.400.10 Alpha Beta Alpha-Beta Complex Oligo-1,6-glucosidase domain 2CATH (4.3.0)
D2.60.40.1180 Mainly Beta Sandwich Immunoglobulin-like Golgi alpha-mannosidase IICATH (4.3.0)
E3.20.20.80 Alpha Beta Alpha-Beta Barrel TIM Barrel GlycosidasesCATH (4.3.0)
E3.90.400.10 Alpha Beta Alpha-Beta Complex Oligo-1,6-glucosidase domain 2CATH (4.3.0)
E2.60.40.1180 Mainly Beta Sandwich Immunoglobulin-like Golgi alpha-mannosidase IICATH (4.3.0)
F3.20.20.80 Alpha Beta Alpha-Beta Barrel TIM Barrel GlycosidasesCATH (4.3.0)
F3.90.400.10 Alpha Beta Alpha-Beta Complex Oligo-1,6-glucosidase domain 2CATH (4.3.0)
F2.60.40.1180 Mainly Beta Sandwich Immunoglobulin-like Golgi alpha-mannosidase IICATH (4.3.0)
G3.20.20.80 Alpha Beta Alpha-Beta Barrel TIM Barrel GlycosidasesCATH (4.3.0)
G3.90.400.10 Alpha Beta Alpha-Beta Complex Oligo-1,6-glucosidase domain 2CATH (4.3.0)
G2.60.40.1180 Mainly Beta Sandwich Immunoglobulin-like Golgi alpha-mannosidase IICATH (4.3.0)
H3.20.20.80 Alpha Beta Alpha-Beta Barrel TIM Barrel GlycosidasesCATH (4.3.0)
H3.90.400.10 Alpha Beta Alpha-Beta Complex Oligo-1,6-glucosidase domain 2CATH (4.3.0)
H2.60.40.1180 Mainly Beta Sandwich Immunoglobulin-like Golgi alpha-mannosidase IICATH (4.3.0)
C3.20.20.80 Alpha Beta Alpha-Beta Barrel TIM Barrel GlycosidasesCATH (4.3.0)
C3.90.400.10 Alpha Beta Alpha-Beta Complex Oligo-1,6-glucosidase domain 2CATH (4.3.0)
C2.60.40.1180 Mainly Beta Sandwich Immunoglobulin-like Golgi alpha-mannosidase IICATH (4.3.0)
O3.90.1200.10 Alpha Beta Alpha-Beta Complex Aminoglycoside 3'-phosphotransferase Chain: A, domain 2CATH (4.3.0)
P3.90.1200.10 Alpha Beta Alpha-Beta Complex Aminoglycoside 3'-phosphotransferase Chain: A, domain 2CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D, E
PF00128Alpha amylase, catalytic domain (Alpha-amylase)Alpha amylase, catalytic domainAlpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, a ...Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
Domain
A, B, C, D, E
PF16657Maltogenic Amylase, C-terminal domain (Malt_amylase_C)Maltogenic Amylase, C-terminal domain- Family
I, J, K, L, M
PF18085Maltokinase N-terminal cap domain (Mak_N_cap)Maltokinase N-terminal cap domainGlycogen is a central energy storage molecule in bacteria and the metabolic pathways associated with its biosynthesis and degradation are crucial for maintaining cellular energy homeostasis. In mycobacteria, the GlgE pathway involves the combined act ...Glycogen is a central energy storage molecule in bacteria and the metabolic pathways associated with its biosynthesis and degradation are crucial for maintaining cellular energy homeostasis. In mycobacteria, the GlgE pathway involves the combined action of trehalose synthase (TreS), maltokinase (Mak) and maltosyltransferase (GlgE). The N-terminal lobe can be divided into two subdomains: a cap N-terminal subdomain comprising the first 88 amino acid residues. This entry is for the cap N-terminal domain found in mycobacterial maltokinase (Mak), (EC:2.7.1.175). The N-terminal cap subdomain and the C-terminal lobe are predominantly acidic, the intermediate subdomain is enriched in positively charged residues. A structural search with only the first 88 amino acid residues of Mak, corresponding to the N-terminal cap subdomain of maltokinases, unveiled a resemblance with proteins displaying the cystatin fold and a remote similarity with the N-terminal domain of the serine/threonine protein kinase GCN2. Conservation of the cap subdomain in maltokinases (including the bifunctional TreS-Mak enzymes), in particular of the residues in the proximity of the P-loop, together with the potential flexibility of this region, are compatible with regulatory functions for this subdomain. Hence it is hypothesised that the N-terminal cap subdomain plays a central role in modulation of Mak enzymatic activity [2].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D, E
Trehalose synthase/amylase TreS -
I, J, K, L, M
Maltokinase -

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B, C, D, E
IPR045857Oligo-1,6-glucosidase, domain 2Homologous Superfamily
A, B, C, D, E
IPR017853Glycoside hydrolase superfamilyHomologous Superfamily
A, B, C, D, E
IPR012810Trehalose synthase/alpha-amylase, N-terminalDomain
A, B, C, D, E
IPR006047Glycosyl hydrolase, family 13, catalytic domainDomain
A, B, C, D, E
IPR013780Glycosyl hydrolase, all-betaHomologous Superfamily
A, B, C, D, E
IPR032091Maltogenic Amylase, C-terminalDomain
I, J, K, L, M
IPR040999Maltokinase N-terminal cap domainDomain
I, J, K, L, M
IPR011009Protein kinase-like domain superfamilyHomologous Superfamily