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CAZyme Information: MGYG000001876_00225

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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 Acetatifactor sp900760705
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp900760705
CAZyme ID MGYG000001876_00225
CAZy Family GT100
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
362 MGYG000001876_3|CGC2 42837.32 6.6928
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001876 3172346 MAG Denmark Europe
Gene Location Start: 66379;  End: 67467  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001876_00225.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT100 113 327 2.5e-42 0.9054054054054054

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07922 Glyco_transf_52 3.00e-07 175 321 102 245
Glycosyltransferase family 52. This family features glycosyltransferases belonging to glycosyltransferase family 52, which have alpha-2,3- sialyltransferase (EC: and alpha-glucosyltransferase (EC 2.4.1.-) activity. For example, beta-galactoside alpha-2,3- sialyltransferase expressed by Neisseria meningitidis is a member of this family and is involved in a step of lipooligosaccharide biosynthesis requiring sialic acid transfer; these lipooligosaccharides are thought to be important in the process of pathogenesis. This family includes several bacterial lipooligosaccharide sialyltransferases similar to the Haemophilus ducreyi LST protein. Haemophilus ducreyi is the cause of the sexually transmitted disease chancroid and produces a lipooligosaccharide (LOS) containing a terminal sialyl N-acetyllactosamine trisaccharide.
pfam07388 A-2_8-polyST 3.68e-04 135 299 119 267
Alpha-2,8-polysialyltransferase (POLYST). This family contains the bacterial enzyme alpha-2,8-polysialyltransferase (EC:2.4.99.-) (approximately 500 residues long). This catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA).
cd04583 CBS_pair_ABC_OpuCA_assoc 0.005 205 283 15 88
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA. This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNM02131.1 4.10e-210 1 362 1 361
QDB89934.1 2.10e-30 5 344 4 318
QHO93504.1 3.59e-22 1 320 3 279
ARC45105.1 3.59e-22 1 320 3 279
CZT39441.1 3.59e-22 1 320 3 279

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P44066 1.22e-07 219 328 168 274
Uncharacterized protein HI_0871 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0871 PE=4 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

1.000045 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001876_00225.