CAZyme Information: MGYG000003736_02787

Basic Information

• Species: Cupriavidus metallidurans
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Cupriavidus; Cupriavidus metallidurans
• CAZyme ID: MGYG000003736_02787
• CAZy Family: GT4
• CAZyme Description: Glutamate/aspartate import solute-binding protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
302	MGYG000003736_56|CGC1	33137.18	9.3802

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003736	3680628	MAG	Canada	North America

• Gene Location: Start: 13808; End: 14716 Strand: +

Full Sequence      

MKSLSVRPTPVTRLLAAAALLCAAAGAHAADGDTLKKIKDSGVISLGYRESSIPFSYSDG
KEVMGYSHDYLLAIVDKVKATLNMPNLQVKLTPITSQNRIPLMQNGTIDIECGSTTNNLE
RQKQVAFSNSLFIYGIRMLTKKDSGVTDFPQLKDKNVVTTAGTTGERLLVKMNGEGMNMN
LTSAKDHGQAFLILESGRAAAFVMDEPLLYGERTKAKNAAEWVVAGKPLQTENYACMFRK
DDPSFKKLVDGVVADIMTSGRGEKLYAKWFQSPIPPRNINMNYPLSPDMKQLFAEPNDKA
FQ

Enzyme Prediction     

No EC number prediction in MGYG000003736_02787.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10797	PRK10797	9.22e-146	32	300	30	300	glutamate and aspartate transporter subunit; Provisional
cd13688	PBP2_GltI_DEBP	5.40e-102	35	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	5.62e-61	35	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	1.33e-60	35	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	1.75e-52	44	270	1	223	Bacterial extracellular solute-binding proteins, family 3.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QXX81055.1	3.65e-114	34	300	27	295
BBV05439.1	5.18e-114	34	300	27	295
QIF58808.1	5.18e-114	34	300	27	295
AWS50894.1	5.18e-114	34	300	27	295
QZY63525.1	5.18e-114	34	300	27	295

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VHA_A	7.73e-115	30	300	5	277	DEBP[Shigella flexneri],2VHA_B DEBP [Shigella flexneri]
2IA4_A	9.09e-109	30	300	5	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	5.02e-20	30	270	3	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]
4YMX_A	1.42e-16	33	271	28	259	ChainA, ABC-type amino acid transport system, periplasmic component [Caldanaerobacter subterraneus subsp. tengcongensis MB4],4YMX_B Chain B, ABC-type amino acid transport system, periplasmic component [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
2YJP_A	1.23e-14	34	268	47	273	Crystalstructure of the solute receptors for L-cysteine of Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090],2YJP_B Crystal structure of the solute receptors for L-cysteine of Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090],2YJP_C Crystal structure of the solute receptors for L-cysteine of Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37902	1.85e-116	7	300	5	300	Glutamate/aspartate import solute-binding protein OS=Escherichia coli (strain K12) OX=83333 GN=gltI PE=1 SV=2
Q9ZF60	8.14e-113	27	300	20	300	Glutamate/aspartate import solute-binding protein OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=gltI PE=3 SV=3
Q9I402	1.10e-105	18	300	14	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	1.30e-21	18	271	14	268	ABC transporter glutamine-binding protein GlnH OS=Bacillus subtilis (strain 168) OX=224308 GN=glnH PE=2 SV=1
P27676	1.75e-17	33	247	50	257	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
0.000599	0.971130	0.027438	0.000296	0.000269	0.000242

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003736_02787.