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CAZyme Information: FPRN_12925-t42_1-p1

You are here: Home > Sequence: FPRN_12925-t42_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Fusarium proliferatum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
CAZyme ID FPRN_12925-t42_1-p1
CAZy Family GH74
CAZyme Description probable beta-galactosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1002 FCQG01000033|CGC3 110357.58 9.3860
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FproliferatumNRRL62905 15602 N/A 348 15254
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.23:18 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH35 49 378 1.2e-92 0.9804560260586319

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396048 Glyco_hydro_35 3.95e-104 47 378 1 313
Glycosyl hydrolases family 35.
402180 BetaGal_dom2 1.56e-72 398 564 9 180
Beta-galactosidase, domain 2. This is the second domain of the five-domain beta-galactosidase enzyme that altogether catalyzes the hydrolysis of beta(1-3) and beta(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and trans-glycosylation. This domain is made up of 16 antiparallel beta-strands and an alpha-helix at its C-terminus. The fold of this domain appears to be unique. In addition, the last seven strands of the domain form a subdomain with an immunoglobulin-like (I-type Ig) fold in which the first strand is divided between the two beta-sheets. In penicillin spp this strand is interrupted by a 12-residue insertion which forms an additional edge-strand to the second beta-sheet of the sub-domain. The remainder of the second domain forms a series of beta-hairpins at its N-terminus, four strands of which are contiguous with part of the Ig-like sub-domain, forming in total a seven-stranded antiparallel beta-sheet. This domain is associated with family Glyco_hydro_35, pfam01301, which is N-terminal to it, but itself has no metazoan members.
198097 BetaGal_dom2 1.83e-60 389 565 1 182
Beta-galactosidase, domain 2. This is the second domain of the five-domain beta-galactosidase enzyme that altogether catalyses the hydrolysis of beta(1-3) and beta(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and trans-glycosylation. This domain is made up of 16 antiparallel beta-strands and an alpha-helix at its C terminus. The fold of this domain appears to be unique. In addition, the last seven strands of the domain form a subdomain with an immunoglobulin-like (I-type Ig) fold in which the first strand is divided between the two beta-sheets. In penicillin spp this strand is interrupted by a 12-residue insertion which forms an additional edge-strand to the second beta-sheet of the sub-domain. The remainder of the second domain forms a series of beta-hairpins at its N terminus, four strands of which are contiguous with part of the Ig-like sub-domain, forming in total a seven-stranded antiparallel beta-sheet. This domain is associated with family Glyco_hydro_35, which is N-terminal to it, but itself has no metazoan members.
166698 PLN03059 1.57e-30 41 364 30 323
beta-galactosidase; Provisional
404274 BetaGal_dom4_5 3.88e-28 853 966 1 111
Beta-galactosidase jelly roll domain. This domain is found in beta galactosidase enzymes. It has a jelly roll fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1002 1 1002
0.0 1 1002 1 1002
0.0 10 1002 418 1410
0.0 10 1002 418 1410
0.0 1 1002 1 1002

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 34 1002 39 1007
STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 3-b-Galactopyranosyl glucose [Aspergillus niger CBS 513.88],5IHR_A Structure Of E298q-beta-galactosidase From Aspergillus Niger In Complex With Allolactose [Aspergillus niger CBS 513.88],5JUV_A STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 6-b-Galactopyranosyl galactose [Aspergillus niger CBS 513.88],5MGC_A STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 4-Galactosyl-lactose [Aspergillus niger CBS 513.88],5MGD_A STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH 6-Galactosyl-lactose [Aspergillus niger CBS 513.88]
0.0 36 1002 1 971
Native structure of beta-galactosidase from Penicillium sp. [Penicillium sp.],1XC6_A Native Structure Of Beta-Galactosidase from Penicillium sp. in complex with Galactose [Penicillium sp.]
0.0 34 1002 39 1007
Structure Of Beta-galactosidase From Aspergillus Niger [Aspergillus niger CBS 513.88]
0.0 24 1002 7 1003
Chain A, Beta-galactosidase [Trichoderma reesei],3OGR_A Chain A, Beta-galactosidase [Trichoderma reesei],3OGS_A Chain A, Beta-galactosidase [Trichoderma reesei],3OGV_A Chain A, Beta-galactosidase [Trichoderma reesei]
0.0 1 1002 1 1005
Crystal structure of beta-galactosidase from Aspergillus oryzae in complex with galactose [Aspergillus oryzae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 34 1002 39 1011
Beta-galactosidase A OS=Penicillium sp. OX=5081 GN=lacA PE=1 SV=1
0.0 34 1002 39 1006
Beta-galactosidase OS=Aspergillus niger OX=5061 GN=lacA PE=1 SV=2
0.0 1 1002 1 1005
Beta-galactosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=lacA PE=1 SV=1
0.0 32 1002 33 1011
Probable beta-galactosidase E OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=lacE PE=3 SV=1
0.0 34 1002 39 1006
Probable beta-galactosidase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=lacA PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000427 0.999532 CS pos: 17-18. Pr: 0.9665

TMHMM  Annotations      help

There is no transmembrane helices in FPRN_12925-t42_1-p1.