CAZyme Information: MGYG000002885_00279

Basic Information

• Species: Pseudomonas_E juntendi
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E juntendi
• CAZyme ID: MGYG000002885_00279
• CAZy Family: GT4
• CAZyme Description: Glutamate/aspartate import solute-binding protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
305	MGYG000002885_15|CGC1	33288.29	8.824

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002885	3148284	MAG	United States	North America

• Gene Location: Start: 7695; End: 8612 Strand: +

Full Sequence      

MRIVRHLLGATIAAAIIASPAMAEELTGTLKKIKDSGTITLGHRDSSIPFSYLAGKPEPV
GYSHDIQLAVVDALKKQLGTDIKVRYNLVTSQTRIPLVQNGTVDLECGSTTNNVERQQQV
GFSVGIFEVGTRLLTKVKDGQPAYKDFPDLAGKNVVTTAGTTSERILKAMNADKQMKMNV
ISAKDHGEAFNMLESGRAVAFMMDDALLAGEMAKARKPADWVITGTPQSYEIYGCMVRKG
DEAFKKAVDDAIVAYFKSGEVNKSYDKWFQQPIPPKGLNLQFPMSDELKKLIAEPTDKAA
DEKKS

Enzyme Prediction     

No EC number prediction in MGYG000002885_00279.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10797	PRK10797	3.58e-141	24	301	23	302	glutamate and aspartate transporter subunit; Provisional
cd13688	PBP2_GltI_DEBP	5.26e-104	30	269	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	1.42e-65	30	269	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	2.46e-63	30	269	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	2.76e-58	39	271	1	225	Bacterial extracellular solute-binding proteins, family 3.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNP18755.1	6.17e-116	1	299	1	295
QLI98284.1	6.17e-116	1	299	1	295
QIF66950.1	6.17e-116	1	299	1	295
BBV05439.1	8.74e-116	1	299	1	295
QIF58808.1	8.74e-116	1	299	1	295

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHA_A	2.90e-108	29	299	9	277	DEBP[Shigella flexneri],2VHA_B DEBP [Shigella flexneri]
2IA4_A	1.68e-102	29	299	9	277	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	2.07e-24	61	269	40	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]
2V25_A	1.45e-13	23	268	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]
2PYY_A	1.78e-13	48	269	12	221	ChainA, Ionotropic glutamate receptor bacterial homologue [Nostoc punctiforme PCC 73102],2PYY_B Chain B, Ionotropic glutamate receptor bacterial homologue [Nostoc punctiforme PCC 73102],2PYY_C Chain C, Ionotropic glutamate receptor bacterial homologue [Nostoc punctiforme PCC 73102]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9I402	3.25e-158	1	302	1	301	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	7.49e-107	29	299	32	300	Glutamate/aspartate import solute-binding protein OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=gltI PE=3 SV=3
P37902	4.29e-106	10	299	9	300	Glutamate/aspartate import solute-binding protein OS=Escherichia coli (strain K12) OX=83333 GN=gltI PE=1 SV=2
O34563	3.82e-25	21	271	30	269	ABC transporter glutamine-binding protein GlnH OS=Bacillus subtilis (strain 168) OX=224308 GN=glnH PE=2 SV=1
P27676	9.68e-18	27	248	49	259	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
0.000528	0.998526	0.000241	0.000244	0.000226	0.000188

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002885_00279.