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CAZyme Information: MGYG000000108_01029

You are here: Home > Sequence: MGYG000000108_01029

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 Citrobacter freundii
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter freundii
CAZyme ID MGYG000000108_01029
CAZy Family GT4
CAZyme Description Glutamate/aspartate import solute-binding protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
302 MGYG000000108_1|CGC10 33423.26 8.424
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000108 4739906 Isolate Canada North America
Gene Location Start: 1077122;  End: 1078030  Strand: +

Full Sequence      Download help

MQLRKLATAM  LVMGMSAGLA  HAEDAAPAAG  STLDKIAKNG  VIVVGHRESS  VPFSYYDNQQ60
KVVGYSQDYS  NAIVEAVKKK  LNKPDLQVKL  IPITSQNRIP  LLQNGTFDFE  CGSTTNNVER120
QKQAAFSDTI  FVVGTRLLAK  KGGDVKDFAD  LKGKAVVVTS  GTTSEVLLHK  LNEEQKMDMR180
IISAKDHGDS  FRTLESGRAV  AFMMDDALLA  GERAKAKKPD  NWEIVGKPQS  QEAYGCMLRK240
DDPEFKKLMD  DTIAKAQTSG  EAEKWFDKWF  KNPIPPKNLN  MNFELSDEMK  ALFKEPNDKA300
LN302

Enzyme Prediction      help

No EC number prediction in MGYG000000108_01029.

CDD Domains      download full data without filtering help

Created with Snap1530456075901051201351511661811962112262412562712861302PRK1079733270PBP2_GltI_DEBP33270PBP2_Cys_DEBP_like33271PBP2_BsGlnH41270PBPb
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10797 PRK10797 0.0 1 302 1 302
glutamate and aspartate transporter subunit; Provisional
cd13688 PBP2_GltI_DEBP 1.84e-119 33 270 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 8.62e-93 33 270 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 2.93e-65 33 271 1 229
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 5.91e-58 41 270 1 219
Bacterial periplasmic substrate-binding proteins. bacterial proteins, eukaryotic ones are in PBPe

CAZyme Hits      help

Created with Snap1530456075901051201351511661811962112262412562712861302QNP18755.1|GT41302QLI98284.1|GT41302QIF66950.1|GT41302BBV05439.1|GT41302QIF58808.1|GT4
Hit ID E-Value Query Start Query End Hit Start Hit End
QNP18755.1 3.25e-169 1 302 1 297
QLI98284.1 3.25e-169 1 302 1 297
QIF66950.1 3.25e-169 1 302 1 297
BBV05439.1 1.88e-168 1 302 1 297
QIF58808.1 1.88e-168 1 302 1 297

PDB Hits      download full data without filtering help

Created with Snap153045607590105120135151166181196211226241256271286243022VHA_A243022IA4_A332775EYF_A402704ZV1_A12652V25_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VHA_A 5.38e-199 24 302 1 279
DEBP[Shigella flexneri],2VHA_B DEBP [Shigella flexneri]
2IA4_A 1.11e-191 24 302 1 279
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 2.49e-28 33 277 8 243
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 5.15e-28 40 270 10 231
Anancestral arginine-binding protein bound to arginine [synthetic construct],4ZV2_A An ancestral arginine-binding protein bound to glutamine [synthetic construct]
2V25_A 6.42e-20 1 265 1 257
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

Created with Snap1530456075901051201351511661811962112262412562712861302sp|Q9ZF60|GLTI_SALTY1302sp|P37902|GLTI_ECOLI5300sp|Q9I402|GASBP_PSEAE32271sp|O34563|GLNH_BACSU31252sp|P27676|GLNH_GEOSE
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9ZF60 2.82e-211 1 302 1 302
Glutamate/aspartate import solute-binding protein OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=gltI PE=3 SV=3
P37902 1.50e-206 1 302 1 302
Glutamate/aspartate import solute-binding protein OS=Escherichia coli (strain K12) OX=83333 GN=gltI PE=1 SV=2
Q9I402 1.74e-114 5 300 2 298
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 2.58e-25 32 271 38 268
ABC transporter glutamine-binding protein GlnH OS=Bacillus subtilis (strain 168) OX=224308 GN=glnH PE=2 SV=1
P27676 4.04e-24 31 252 50 262
Glutamine-binding protein OS=Geobacillus stearothermophilus OX=1422 GN=glnH PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000672 0.900186 0.098094 0.000414 0.000326 0.000267

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000108_01029.