CAZyme Information: MGYG000001708_02662

Basic Information

• Species: Providencia rustigianii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Providencia; Providencia rustigianii
• CAZyme ID: MGYG000001708_02662
• CAZy Family: GT4
• CAZyme Description: Glutamate/aspartate import solute-binding protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
297	MGYG000001708_72|CGC1	32977.87	9.6167

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001708	3896203	Isolate	not provided	not provided

• Gene Location: Start: 34709; End: 35602 Strand: -

Full Sequence      

MRMSKLVLTMMLLGATCAVQAEELNGTLKKIKDNGVIVVGHRESSVPFSYYDNSQKVVGY
SQDYSNQIVDAVKKKLNMPDLQVKLIPITSQNRIPLLQNGTFDFECGSTTNNLERQKQAA
FSNTIFVVGTRLLAKKDAGIKDFADLAGKNVVVTSGTTSEIILNQLNDQKNMKMRIISAK
DHGDSFRTLESGRAVAFMMDDALLAGERAKAKQPAIWEIVGKPQTQEAYGCMLRKDDPQF
KALIDETISTAQKSGTAEKSFNRWFNQPIPPKNLNLNFTLSDEMKALYKSPNDKALN

Enzyme Prediction     

No EC number prediction in MGYG000001708_02662.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10797	PRK10797	0.0	1	297	1	302	glutamate and aspartate transporter subunit; Provisional
cd13688	PBP2_GltI_DEBP	4.30e-115	28	265	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	3.79e-82	28	265	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	2.27e-68	28	265	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	1.62e-58	37	267	1	225	Bacterial extracellular solute-binding proteins, family 3.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VEH54506.1	2.86e-212	1	297	1	297
VEB67078.1	4.74e-211	1	297	1	297
QLR05805.1	5.68e-203	1	297	1	297
SQI32768.1	1.63e-202	1	297	1	297
QLQ98413.1	1.63e-202	1	297	1	297

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHA_A	1.38e-163	21	297	3	279	DEBP[Shigella flexneri],2VHA_B DEBP [Shigella flexneri]
2IA4_A	2.42e-157	21	297	3	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	3.31e-26	28	265	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]
6WUP_A	4.30e-15	28	264	7	235	Crystalstructure of an ancestral cyclohexadienyl dehydratase, AncCDT-5 [synthetic construct]
6MLO_E	2.09e-14	39	266	8	232	Crystalstructure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) Y14A mutant from Salmonella typhimurium complexed with arginine [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],6MLP_E Crystal structure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) Y14A mutant from Salmonella typhimurium complexed with histidine [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],6MLV_A Crystal structure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) Y14A mutant from Salmonella typhimurium [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZF60	1.85e-162	1	297	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	3.05e-161	21	297	26	302	Glutamate/aspartate import solute-binding protein OS=Escherichia coli (strain K12) OX=83333 GN=gltI PE=1 SV=2
Q9I402	3.57e-115	19	295	21	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	1.21e-24	14	267	25	269	ABC transporter glutamine-binding protein GlnH OS=Bacillus subtilis (strain 168) OX=224308 GN=glnH PE=2 SV=1
P27676	1.32e-20	27	247	51	262	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
0.000337	0.998853	0.000286	0.000178	0.000169	0.000156

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001708_02662.