CAZyme Information: MGYG000000150_06336

Basic Information

• Species: Hungatella sp005845265
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Hungatella; Hungatella sp005845265
• CAZyme ID: MGYG000000150_06336
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1490	MGYG000000150_53|CGC1	173661.48	5.6652

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000150	7470188	Isolate	United Kingdom	Europe

• Gene Location: Start: 19092; End: 23564 Strand: -

Full Sequence      

MNQLINSEEYWDKRFQTDWDKYSGEEQTEFFAEITCRLLPAWLVKSIRMNKYIICDMGCA
CGEAVNILSQYLNTKVCGMDFANSAIEIAKKKYPIYQFEQGDISTLDTGKKIDIVYCSNV
LEHFYTPWDMAEKMAMVTKHYLILQMPFREQLTIDEHFFKFDTNIIPLQIGEFTLVNLET
VNGSEIPGTLYPDQQVLLVYSSHKEDIITARIDDIYKGIKNSDLIQWNNQKKEIEEYYNV
QIAELKNTLEKLNTDYSLVSDEFNKRGLLIETSSKQLTDQIRTNSLLQEEIQNQKKLMTS
LTQENNETIGKLTKANSSLQDEIQSHKKKLATYAEKNKEIAKELAEYRNNYNLLKEEIKD
LKSIKEKYATLLLEKKQLDKELQNKESIIHRAKQKCVYMASTKTFRTVHFMFRLKYQFLK
GTKDERKSFGKWLKSELCQKGGDSERRYNPIWNVISILDEVSGAKINSTLKVTDDIMLSN
APLAKHLQEEQQRLVSNIDLNSNEYMAIKEVLNSNKDMRIMIYPHVVYWEPLQTPQQLLK
AFANNGWLCFFCEHPSLQNIYREAYPGLFIVHEKELLQAIDNREVFVLLTWLGSLSFINQ
IANKQIWYHILDKLDLFPYYDKYYDKLHTTIVRQASFVSYVASPLLNCLENRRDPIYLPN
AVNPEDFLNIHNNYVPEDMKPILSKKHKIIGYYGYLAEWLDYELVRELAAARPNYEFVFI
GKAIYDTSEIDNLSNVHLLGLKPYKELSDYAKYFDVATIPFIINDKMDCVSPIKFFEYCA
LGLPVVTSSMKEMDNFVCDFIACANGVDEFLFYLDKMVTKECHDLAIENGPLIALQNTWN
SRIKIMEDVFNQELQNILNSDYENFDVILLGVIDFDYRYQRPQHFASRFAENGHRVFYVN
ANHFNPDSVVRICNDLYVINIYNDQSTAIHLTDWHEQLSLLHEKLDKIMNTYCIRDAVVI
VDYPNWIFTAEHLRNLYGFKIITDYMDDFTGFLNPAESLVKENCKKLLELSDYVVASSEF
LYDIAKKFNKNIEIIRNGTEYAHFHKAAVEHKNERKIIGYYGAVAEWFDYSKVIYVAQNM
PDCDVVIIGRVTAGEKQLSKYNNIKLLGEIPYNELPKYLECFDVCLIPFDTSTDLIKATN
PVKFYEYLSAGKKIVATDIPELEPFKDKYVYLSNDNHQFLEYIKICLENKDCLANDTEKM
AFALKNDWQIRYENFYEVCRRAVPKVSIIVLTYNNLEINKICMNSILHNTAYANYELIVV
DNCSTDGTTDYLRTLERDDARVKLILNKENKGFAGGNNVGINASSGEYVLLLNNDTVVTR
GWITAMAKHLENNSKLGMCGPVTNSIGNEAKIKVNYHSVKEMYSFAYRYTTDHLNSEYKN
PNVLALFCTMIKRNVIDSCGLLDEMYEIGMFEDDDYAEAVKQKGYELAIAEDAFIHHFEG
ASFKKLEDKKFHDIYDQNKERFEKKWGKKWTMHKKRKGITWDTNSEVNIL

Enzyme Prediction     

No EC number prediction in MGYG000000150_06336.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1227	1397	3.8e-28	0.9764705882352941

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04950	GT4_TuaH-like	4.27e-56	863	1213	3	363	teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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.
cd04950	GT4_TuaH-like	9.75e-45	583	853	102	372	teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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.
cd04186	GT_2_like_c	8.00e-39	1228	1439	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.
COG1216	GT2	1.34e-37	1224	1451	3	233	Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism].
cd00761	Glyco_tranf_GTA_type	1.01e-25	1228	1346	1	118	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
BCN32217.1	0.0	1	1489	1	1477
AOY75534.1	3.22e-203	820	1479	483	1140
ARE85828.1	3.22e-203	820	1479	483	1140
AEG59392.1	2.69e-145	816	1473	298	963
QDT93025.1	1.45e-141	854	1473	247	867

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O32267	1.79e-13	973	1208	120	380	Putative teichuronic acid biosynthesis glycosyltransferase TuaH OS=Bacillus subtilis (strain 168) OX=224308 GN=tuaH PE=2 SV=1
Q57287	2.94e-12	1224	1340	5	120	Uncharacterized glycosyltransferase HI_1578 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1578 PE=3 SV=1
P55465	1.97e-11	1222	1442	623	850	Uncharacterized protein y4gI OS=Sinorhizobium fredii (strain NBRC 101917 / NGR234) OX=394 GN=NGR_a03550 PE=4 SV=1
O32268	1.95e-09	1224	1315	6	96	Putative teichuronic acid biosynthesis glycosyltransferase TuaG OS=Bacillus subtilis (strain 168) OX=224308 GN=tuaG PE=2 SV=1
Q0P9C6	3.73e-08	1223	1326	1	104	GalNAc(5)-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pglI 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
1.000038	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000150_06336.