logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001393_04058

You are here: Home > Sequence: MGYG000001393_04058

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 Hafnia paralvei
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Hafnia; Hafnia paralvei
CAZyme ID MGYG000001393_04058
CAZy Family GT4
CAZyme Description Glutamate/aspartate import solute-binding protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
286 MGYG000001393_74|CGC2 31872.28 9.1995
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001393 4880992 Isolate not provided not provided
Gene Location Start: 80812;  End: 81672  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001393_04058.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10797 PRK10797 0.0 1 283 19 299
glutamate and aspartate transporter subunit; Provisional
cd13688 PBP2_GltI_DEBP 1.85e-116 17 254 1 238
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic binding protein fold. This subfamily represents the periplasmic-binding protein component of ABC transporter specific for carboxylic amino acids, including GtlI from Escherichia coli. The aspartate-glutamate binding domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
cd01000 PBP2_Cys_DEBP_like 4.23e-84 17 254 1 228
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold. This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
cd13689 PBP2_BsGlnH 6.44e-65 17 254 1 228
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 periplasmic-bindig protein fold. This group includes periplasmic glutamine-binding domain GlnP from Bacillus subtilis and its related proteins. The GlnP domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
smart00062 PBPb 1.50e-57 25 254 1 219
Bacterial periplasmic substrate-binding proteins. bacterial proteins, eukaryotic ones are in PBPe

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QWJ92671.1 1.29e-164 9 283 20 294
QLQ94799.1 1.29e-164 9 283 20 294
QQE94206.1 1.29e-164 9 283 20 294
QXX81055.1 7.43e-164 9 283 20 294
QNP18755.1 1.50e-163 9 283 20 294

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHA_A 8.06e-167 12 283 5 276
DEBP[Shigella flexneri],2VHA_B DEBP [Shigella flexneri]
2IA4_A 1.65e-159 12 283 5 276
Crystalstructure of Novel amino acid binding protein from Shigella flexneri [Shigella flexneri 2a str. 301],2IA4_B Crystal structure of Novel amino acid binding protein from Shigella flexneri [Shigella flexneri 2a str. 301]
5EYF_A 4.52e-29 10 254 1 236
CrystalStructure of Solute-binding Protein from Enterococcus faecium with Bound Glutamate [Enterococcus faecium DO],5EYF_B Crystal Structure of Solute-binding Protein from Enterococcus faecium with Bound Glutamate [Enterococcus faecium DO]
4ZV1_A 3.90e-26 24 256 10 233
Anancestral arginine-binding protein bound to arginine [synthetic construct],4ZV2_A An ancestral arginine-binding protein bound to glutamine [synthetic construct]
2V25_A 4.48e-18 10 249 24 257
Structureof the Campylobacter jejuni antigen Peb1A, an aspartate and glutamate receptor with bound aspartate [Campylobacter jejuni],2V25_B Structure of the Campylobacter jejuni antigen Peb1A, an aspartate and glutamate receptor with bound aspartate [Campylobacter jejuni]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9ZF60 5.60e-168 1 283 19 299
Glutamate/aspartate import solute-binding protein OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=gltI PE=3 SV=3
P37902 3.08e-165 7 283 23 299
Glutamate/aspartate import solute-binding protein OS=Escherichia coli (strain K12) OX=83333 GN=gltI PE=1 SV=2
Q9I402 3.15e-113 10 286 23 300
L-glutamate/L-aspartate-binding protein OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=PA1342 PE=1 SV=1
O34563 1.79e-26 7 256 29 269
ABC transporter glutamine-binding protein GlnH OS=Bacillus subtilis (strain 168) OX=224308 GN=glnH PE=2 SV=1
P27676 2.91e-21 5 236 40 262
Glutamine-binding protein OS=Geobacillus stearothermophilus OX=1422 GN=glnH PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001393_04058.