CAZyme Information: MGYG000001384_01264

Basic Information

• Species: Ralstonia pickettii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Ralstonia; Ralstonia pickettii
• CAZyme ID: MGYG000001384_01264
• CAZy Family: GT4
• CAZyme Description: Glutamate/aspartate import solute-binding protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
302	MGYG000001384_1|CGC9	32956.98	9.7055

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001384	5243975	Isolate	not provided	not provided

• Gene Location: Start: 1315035; End: 1315943 Strand: -

Full Sequence      

MNLAKLATVVAAVGVAVGAFGSAAHAEELTGTLKKIKDTGTITLGVRDSSIPFSYNVGGV
RTIGYSYDVATKIAEDVKKQLGLKDLKVNEIPVTSQNRITLLQNGTIDLECGSTTNNLER
QKQASFTNTIFIIGTRIMVKKDSGVKDWADLKGKNVVTTAGTTSERLLRKMNDEKQMGMN
IISTKDHGQSFLTLESGRAVAFMMDDALLYGERAKAKNPAEWVVVAKPQSREAYGCMVRK
DDKPFKALADKTIAGMMKDGTINAEYKKWFEQPVPPKGVNMEFPLSDDMKALIKNPNDKA
LD

Enzyme Prediction     

No EC number prediction in MGYG000001384_01264.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10797	PRK10797	2.29e-154	22	302	18	302	glutamate and aspartate transporter subunit; Provisional
cd13688	PBP2_GltI_DEBP	2.77e-107	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	3.20e-68	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	6.87e-67	33	270	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.
pfam00497	SBP_bac_3	5.07e-57	42	270	1	223	Bacterial extracellular solute-binding proteins, family 3.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLR05805.1	1.01e-130	23	301	18	296
VEH54506.1	1.44e-130	23	301	18	296
VEB67078.1	1.44e-130	23	301	18	296
SQI32768.1	2.04e-130	23	301	18	296
QLQ98413.1	2.04e-130	23	301	18	296

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHA_A	6.15e-119	32	301	9	278	DEBP[Shigella flexneri],2VHA_B DEBP [Shigella flexneri]
2IA4_A	1.46e-112	32	301	9	278	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]
4ZV1_A	1.04e-26	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]
5EYF_A	3.79e-23	33	270	8	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]
5T0W_A	5.44e-22	32	271	15	246	Crystalstructure of the ancestral amino acid-binding protein AncCDT-1, a precursor of cyclohexadienyl dehydratase [synthetic construct],5T0W_B Crystal structure of the ancestral amino acid-binding protein AncCDT-1, a precursor of cyclohexadienyl dehydratase [synthetic construct],5T0W_C Crystal structure of the ancestral amino acid-binding protein AncCDT-1, a precursor of cyclohexadienyl dehydratase [synthetic construct],5T0W_D Crystal structure of the ancestral amino acid-binding protein AncCDT-1, a precursor of cyclohexadienyl dehydratase [synthetic construct]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9I402	4.47e-122	26	300	23	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
Q9ZF60	1.20e-119	1	301	1	301	Glutamate/aspartate import solute-binding protein OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=gltI PE=3 SV=3
P37902	5.63e-118	1	301	1	301	Glutamate/aspartate import solute-binding protein OS=Escherichia coli (strain K12) OX=83333 GN=gltI PE=1 SV=2
O34563	2.43e-28	16	272	20	269	ABC transporter glutamine-binding protein GlnH OS=Bacillus subtilis (strain 168) OX=224308 GN=glnH PE=2 SV=1
P27676	1.08e-24	30	245	49	255	Glutamine-binding protein OS=Geobacillus stearothermophilus OX=1422 GN=glnH PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000307	0.998889	0.000239	0.000189	0.000196	0.000172

TMHMM  Annotations     

start	end
7	26