CAZyme Information: MGYG000000137_01818

Basic Information

• Species: UBA7160 sp902363665
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA7160; UBA7160 sp902363665
• CAZyme ID: MGYG000000137_01818
• CAZy Family: GT4
• CAZyme Description: Glycosyltransferase Gtf1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
978	MGYG000000137_7|CGC4	109314.01	6.7621

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000137	4141348	Isolate	United Kingdom	Europe

• Gene Location: Start: 205937; End: 208873 Strand: +

Full Sequence      

MSFDKKKLVKIIKTTAMAMAVAFAGLCFISKKKKSATVYENEPEQKNPLEGKKVVFVEDE
SEPENADGARGHLEAVGDSDYRPGFYEKCIKRALDVILSFGGLVVLSPIYAGIALAIVID
DPGPVLFTQKRMGQNKKYFKLHKFRSMKMSTPHDVPTHMLDNPEQYITRVGKFLRAHSLD
ELPQIWDIFVGNMSVIGPRPGLWNQDILTAERDKYNANDVKPGLTGWAQINGRDELEIPV
KAKLDGEYVKKMGPLMDLKCFLGSVGVFAHDDSVVEGGTGEMKKAVGRHYTDGKTAEELI
GHIGFGEPVEVDTETKKKVLITGAGSYIGETFRAYAAEHYPALEIDAVDMLDASWREKDF
SEYDIVYHVAGIAHADVGNVDEATKAKYYAVNTDLAVEVCEKAKAEGVKEFVFMSSMIVY
GDSAPYGKKKVVDEHTVPKAANFYGDSKLQADVAVRGLADDDFKVIVLRPPMIYGKGSKG
NYPTLAKLAKKLPVFPNVDNERSMLHINNLCEFLCQIMLVKEVKENAIVLIPQNGEWTKT
SEMVKEIGEVSGKKVRLVGGIMKPAVWIGGKVPGKIGGMVNKAFGNSVYKHEISLYSGVD
YQNISLKESIKMTESNSEKKKVLFLVNHDVVIYNFRLELVERLLDDGYEVHISSPYGERI
DELKELGAIFHEINMDRHGMNPISEGKLLLNYRKLLAEVKPDIILGYTIKPNIYGAMAAS
EKNIPFVANITGLGTAVENPGMSQKLMVLLYKIAFRKVQKVFFQNKENQQFFIAHNIAIG
KQGLLPGSGVNLTRFAVEDYPKDDIVRFAFISRIMKEKGIDQYLDAAKFIKEKYPNTEFH
VCGFCEKEYEGKLNEYNDNGTVIYHGMIHDVAGFLENMNCVVHPTYYPEGLSNVLLEASA
CGRPIITTDRSGCREVVDDGINGYMIPQKNSEKLIEAIDRFMNLSYEEKRGMGLAARKKV
EENFDRSIVVEAYMREIK

Enzyme Prediction     

No EC number prediction in MGYG000000137_01818.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	808	950	5.5e-28	0.90625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03808	GT4_CapM-like	1.44e-116	621	974	1	358	capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
pfam02397	Bac_transf	1.36e-70	91	267	1	178	Bacterial sugar transferase. This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways.
COG2148	WcaJ	1.77e-66	90	265	40	216	Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis].
cd05232	UDP_G4E_4_SDR_e	1.40e-58	318	613	1	303	UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
TIGR03025	EPS_sugtrans	4.47e-53	90	259	257	429	exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase. Members of this family are generally found near other genes involved in the biosynthesis of a variety of exopolysaccharides. These proteins consist of two fused domains, an N-terminal hydrophobic domain of generally low conservation and a highly conserved C-terminal sugar transferase domain (pfam02397). Characterized and partially characterized members of this subfamily include Salmonella WbaP (originally RfbP), E. coli WcaJ, Methylobacillus EpsB, Xanthomonas GumD, Vibrio CpsA, Erwinia AmsG, Group B Streptococcus CpsE (originally CpsD), and Streptococcus suis Cps2E. Each of these is believed to act in transferring the sugar from, for instance, UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate as the first (priming) step in the synthesis of an oligosaccharide "block". This function is encoded in the C-terminal domain. The liposaccharide is believed to be subsequently transferred through a "flippase" function from the cytoplasmic to the periplasmic face of the inner membrane by the N-terminal domain. Certain closely related transferase enzymes, such as Sinorhizobium ExoY and Lactococcus EpsD, lack the N-terminal domain and are not found by this model.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUO31262.1	0.0	1	925	1	960
QMW80818.1	1.79e-180	90	975	34	1022
QIB56408.1	1.79e-180	90	975	34	1022
QQY28407.1	2.35e-170	620	977	2	359
QQV06535.1	2.32e-167	620	977	2	359

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5W7L_A	7.40e-30	84	289	4	205	Structureof Campylobacter concisus PglC I57M/Q175M variant [Campylobacter concisus 13826],5W7L_B Structure of Campylobacter concisus PglC I57M/Q175M variant [Campylobacter concisus 13826]
7EC2_A	2.14e-12	642	943	151	458	ChainA, Glycosyl transferase, group 1 family protein [Staphylococcus aureus subsp. aureus USA300],7EC2_B Chain B, Glycosyl transferase, group 1 family protein [Staphylococcus aureus subsp. aureus USA300]
1HZJ_A	3.93e-08	323	555	41	292	HumanUdp-Galactose 4-Epimerase: Accommodation Of Udp-N- Acetylglucosamine Within The Active Site [Homo sapiens],1HZJ_B Human Udp-Galactose 4-Epimerase: Accommodation Of Udp-N- Acetylglucosamine Within The Active Site [Homo sapiens]
1I3K_A	9.20e-08	323	555	41	292	ChainA, UDP-GLUCOSE 4-EPIMERASE [Homo sapiens],1I3K_B Chain B, UDP-GLUCOSE 4-EPIMERASE [Homo sapiens],1I3L_A Chain A, UDP-GLUCOSE 4-EPIMERASE [Homo sapiens],1I3L_B Chain B, UDP-GLUCOSE 4-EPIMERASE [Homo sapiens],1I3M_A Chain A, UDP-GLUCOSE 4-EPIMERASE [Homo sapiens],1I3M_B Chain B, UDP-GLUCOSE 4-EPIMERASE [Homo sapiens],1I3N_A Chain A, UDP-GLUCOSE 4-EPIMERASE [Homo sapiens],1I3N_B Chain B, UDP-GLUCOSE 4-EPIMERASE [Homo sapiens]
1EK5_A	1.22e-07	323	555	41	292	StructureOf Human Udp-galactose 4-epimerase In Complex With Nad+ [Homo sapiens],1EK6_A Structure Of Human Udp-galactose 4-epimerase Complexed With Nadh And Udp-glucose [Homo sapiens],1EK6_B Structure Of Human Udp-galactose 4-epimerase Complexed With Nadh And Udp-glucose [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0P9C9	2.49e-30	621	975	2	367	N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pglA PE=1 SV=1
Q0P9D0	8.91e-29	86	277	2	189	Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pglC PE=1 SV=1
P71241	1.08e-28	88	259	271	448	UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase OS=Escherichia coli (strain K12) OX=83333 GN=wcaJ PE=1 SV=2
P10498	6.67e-27	90	265	5	190	Exopolysaccharide production protein PSS OS=Rhizobium leguminosarum bv. phaseoli OX=385 GN=pss PE=3 SV=1
Q44576	7.63e-26	91	259	338	516	Undecaprenyl-phosphate glucose phosphotransferase OS=Komagataeibacter xylinus OX=28448 GN=aceA PE=3 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
0.980814	0.018403	0.000479	0.000111	0.000060	0.000151

TMHMM  Annotations     

start	end
11	30
96	118