CAZyme Information: MGYG000001423_00185

Basic Information

• Species: Clostridium celatum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium celatum
• CAZyme ID: MGYG000001423_00185
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
301	MGYG000001423_7|CGC1	34864.09	9.5346

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001423	3553421	Isolate	not provided	not provided

• Gene Location: Start: 9100; End: 10005 Strand: -

Full Sequence      

MLGIVIANWNGEKLIDKCLTSLKNQEFKEFKIYIIDNDSRDNSRNIINGYKNELDIDLIE
MDYNSGFAPANNIGIKKARNDGCEYILTLNNDVEVPKESLKNAISLIKTNKDYDVFQLFM
INYFEREKCDAAGLTFDKKLLPAQVGYRENVKEVLKRDINIEGACAGAAIYTKKALEKVK
LQNGDYFDSKFFAYYEDVDLSLRLKRAGFKSKLLKDSIVYHMHSATGNKTSGFKEYYLAR
NLFMYTKRNQPIENYKKAKNTYYRILIKNMIKNFNSDVMKSVLKGIKDGNKEAKNIEYKP
Y

Enzyme Prediction     

No EC number prediction in MGYG000001423_00185.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	4	179	9.3e-26	0.9823529411764705

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1216	GT2	1.89e-45	1	275	4	266	Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism].
cd04186	GT_2_like_c	9.29e-42	4	223	1	166	Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
pfam00535	Glycos_transf_2	2.49e-22	4	176	2	164	Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
cd04185	GT_2_like_b	3.18e-18	5	243	2	200	Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
cd00761	Glyco_tranf_GTA_type	5.33e-17	4	115	1	110	Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLY79136.1	1.61e-117	1	289	1	289
AYE34882.1	1.93e-85	1	288	1	267
QAS60277.1	3.80e-83	34	288	1	258
AMV73141.1	4.17e-45	3	251	12	262
BCS54874.1	1.91e-43	1	251	7	248

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5TZE_C	5.45e-10	3	107	4	108	Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus]
5TZ8_A	7.46e-10	3	107	4	108	Crystalstructure of S. aureus TarS [Staphylococcus aureus],5TZ8_B Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_C Crystal structure of S. aureus TarS [Staphylococcus aureus]
3L7I_A	2.61e-06	2	95	4	96	Structureof the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_B Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_C Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_D Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A]
3L7J_A	2.61e-06	2	95	4	96	ChainA, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_A Chain A, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_A Chain A, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A]
3L7M_A	2.61e-06	2	95	4	96	ChainA, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A0H3JPC6	4.09e-09	3	107	5	109	Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=tarS PE=1 SV=1
A0A0H3JVA1	4.09e-09	3	107	5	109	Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS OS=Staphylococcus aureus (strain MW2) OX=196620 GN=tarS PE=1 SV=1
E0U4V7	1.84e-07	2	208	3	209	Poly(ribitol-phosphate) beta-glucosyltransferase OS=Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) OX=655816 GN=tarQ PE=1 SV=1
Q5HKQ0	8.40e-06	2	110	49	154	Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=icaA PE=1 SV=1

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
1.000050	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001423_00185.