Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1o08a_ Alpha and beta proteins (a/b) HAD-like HAD-like beta-Phosphoglucomutase-like beta-Phosphoglucomutase (Lactococcus lactis ) [TaxId: 1358 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 Familybeta-Phosphoglucomutase-like 8021421 4002304 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyHAD-like 8033801 3001890 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AHAD_2e1o08A1 A: a/b three-layered sandwichesX: HAD domain-likeH: HAD domain-relatedT: HAD-likeF: HAD_2ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.50.1000 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold HAD superfamily/HAD-likeCATH (4.3.0)
A1.10.150.240 Mainly Alpha Orthogonal Bundle DNA polymerase domain 1CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00702haloacid dehalogenase-like hydrolase (Hydrolase)haloacid dehalogenase-like hydrolaseThis family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted fo ...This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain [1]. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria [2].
Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
beta-phosphoglucomutase  M-CSA #206

This enzyme catalyses the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. It requires Mg(II) and phosphorylation of an aspartate residue at the active site. The enzyme is able to autophosphorylate itself with its substrate beta-D-glucose 1-phosphate. Although this is a slow reaction, only a single turnover is required for activation. Once the phosphorylated enzyme is formed, it generates the reaction intermediate beta-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles [PMID:16784233].

Defined by 10 residues: ASP:A-8 [auth A-1008]LEU:A-9 [auth A-1009]ASP:A-10 [auth A-1010]THR:A-16 [auth A-1016]LYS:A-45 [auth A-1045]SER:A-114 [auth A-1114]ALA:A-115 [auth A-1115]LYS:A-145 [auth A-1145]GLU:A-169 [auth A-1169]ASP:A-170 [auth A-1170]
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