CAZyme Information: MGYG000001216_00139

Basic Information

• Species: CAG-354 sp900759015
• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-354; CAG-354 sp900759015
• CAZyme ID: MGYG000001216_00139
• CAZy Family: GT51
• CAZyme Description: Monofunctional glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
232	MGYG000001216_1|CGC1	26437.56	4.8389

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001216	1847143	MAG	Austria	Europe

• Gene Location: Start: 121483; End: 122181 Strand: -

Full Sequence      

MKTFLKVILLLMLIGISIGLLLIGKGYDMYKEAIQETPLEEKVEEIKSKANYTKISELPQ
MYLDAVISVEDHRFYKHSGIDIIAIGRALINDIKAMEFVEGGSTITQQIAKNEYFTQEKK
ITRKIAEVFMAYEIEKNYSKDEILELYINTIYFGNGYYNIKDACKGYFGKSPNEMTAGEC
IMLAGIPNAPSVYNPKENPKLAKERQKQVADKMVEYGYLTEEEEAEILNSGF

Enzyme Prediction     

No EC number prediction in MGYG000001216_00139.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	46	214	1.2e-63	0.9548022598870056

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	6.32e-83	52	214	15	177	Transglycosylase. The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.
TIGR02074	PBP_1a_fam	1.08e-81	52	230	4	182	penicillin-binding protein, 1A family. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
COG0744	MrcB	2.25e-74	1	230	8	257	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	2.51e-70	1	223	1	240	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK13481	PRK13481	3.57e-49	4	228	8	229	glycosyltransferase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM09777.1	9.40e-89	6	228	19	241
QJU22158.1	8.61e-88	25	231	28	234
QRP41835.1	1.22e-87	25	231	28	234
ASN93505.1	1.22e-87	25	231	28	234
QIX92252.1	2.84e-86	25	231	28	234

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	7.49e-46	49	229	19	199	Crystalstructure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis [Aquifex aeolicus VF5],3D3H_A Crystal structure of a complex of the peptidoglycan glycosyltransferase domain from Aquifex aeolicus and neryl moenomycin A [Aquifex aeolicus],3NB7_A Crystal structure of Aquifex Aeolicus Peptidoglycan Glycosyltransferase in complex with Decarboxylated Neryl Moenomycin [Aquifex aeolicus]
3NB6_A	2.99e-45	49	229	19	199	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
3UDF_A	1.25e-40	57	223	46	212	ChainA, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDF_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii]
4OON_A	4.71e-39	54	222	43	211	Crystalstructure of PBP1a in complex with compound 17 ((4Z,8S,11E,14S)-5-(2-amino-1,3-thiazol-4-yl)-14-(5,6-dihydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-8-formyl-2-methyl-6-oxo-3,10-dioxa-4,7,11-triazatetradeca-4,11-diene-2,12,14-tricarboxylic acid) [Pseudomonas aeruginosa PAO1]
5U2G_A	8.14e-38	54	223	44	213	2.6Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20],5U2G_B 2.6 Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q07259	5.61e-47	51	220	48	216	Putative transglycosylase H16_A0665 OS=Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) OX=381666 GN=H16_A0665 PE=3 SV=2
O87626	5.52e-45	47	220	65	238	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA PE=3 SV=1
Q5FAC7	1.95e-44	47	229	65	247	Penicillin-binding protein 1A OS=Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) OX=242231 GN=mrcA PE=3 SV=3
P0A0Z6	1.95e-44	47	229	65	247	Penicillin-binding protein 1A OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=mrcA PE=3 SV=1
P0A0Z5	1.95e-44	47	229	65	247	Penicillin-binding protein 1A OS=Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491) OX=122587 GN=mrcA 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
0.945534	0.045818	0.006871	0.000201	0.000122	0.001482

TMHMM  Annotations     

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