CAZyme Information: MGYG000000418_01704

Basic Information

• Species: UBA1820 sp003150615
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; UBA1820; UBA1820; UBA1820 sp003150615
• CAZyme ID: MGYG000000418_01704
• CAZy Family: GT9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
344	MGYG000000418_12|CGC1	38811.22	9.5645

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000418	2050770	MAG	Sweden	Europe

• Gene Location: Start: 29958; End: 30992 Strand: +

Full Sequence      

MKHLLVLRISAFGDVALAIPVVREFLQQHPDVRITFVSSPAFADIFKGIDRLEFFPVYVH
GRHKGPLGMVRLVSDLLKKDRYDAVLDLHSVIRTHMMRFLFHMRFVPVYKMYKIREERKR
LTRKDNKIKSPIKPIPECYADVFRRAGYTVTLSNKLSPRPREVKPSTLEKVGGRRDSVWI
GIAPFSQYTGKSYPLDRMFEAVKNIARFKNADIFLFGAPGAEAETLKNWSQSLDNVHTVA
GSVSLGEELDIISNLRVMVSMDSANMHLASLMGVRVISVWGATHHFAGFLGYGQSADDII
GAEMDCRPCSVFGNKECWKGTYECMTAIQPELIACKVEEAAGLP

Enzyme Prediction     

No EC number prediction in MGYG000000418_01704.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT9	76	319	5.8e-34	0.9377777777777778

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03789	GT9_LPS_heptosyltransferase	2.32e-45	3	341	1	275	lipopolysaccharide heptosyltransferase and similar proteins. Lipopolysaccharide heptosyltransferase (2.4.99.B6) is involved in the biosynthesis of lipooligosaccharide (LOS). Lipopolysaccharide (LPS) is a major component of the outer membrane of gram-negative bacteria. LPS heptosyltransferase transfers heptose molecules from ADP-heptose to 3-deoxy-D-manno-octulosonic acid (KDO), a part of the inner core component of LPS. This family also contains lipopolysaccharide 1,2-N-acetylglucosaminetransferase EC 2.4.1.56 and belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
COG0859	RfaF	5.75e-40	1	333	1	322	ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis].
pfam01075	Glyco_transf_9	3.80e-12	77	316	8	243	Glycosyltransferase family 9 (heptosyltransferase). Members of this family belong to glycosyltransferase family 9. Lipopolysaccharide is a major component of the outer leaflet of the outer membrane in Gram-negative bacteria. It is composed of three domains; lipid A, Core oligosaccharide and the O-antigen. All of these enzymes transfer heptose to the lipopolysaccharide core.
cd08422	PBP2_CrgA_like	4.53e-05	6	50	2	49	The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 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 cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
cd08474	PBP2_CrgA_like_5	7.90e-05	7	45	5	45	The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 5. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 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 cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SDT21404.1	9.88e-96	2	339	5	340
ASU33781.1	1.40e-95	2	339	5	340
QWG06526.1	1.03e-93	2	340	3	344
AZQ63461.1	1.33e-91	2	340	3	344
ANQ50106.2	1.52e-90	2	333	3	337

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000000	0.000047	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000418_01704.