CAZyme Information: MGYG000001256_00960

Basic Information

• Species: CAG-354 sp001915925
• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-354; CAG-354 sp001915925
• CAZyme ID: MGYG000001256_00960
• CAZy Family: GT51
• CAZyme Description: Monofunctional glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
229		26099.68	4.4009

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001256	1702469	MAG	Austria	Europe

• Gene Location: Start: 118347; End: 119036 Strand: -

Full Sequence      

MKKFLLILLLILILTAASLGIYGYSLYSQAIKKEPLISKIEQIQSDENYVKYENLPQDYL
DAVVSVEDRRFYDHGAIDLRSIARAIYVNVTNFDLREGGSTITQQLAKNIYFIDMNPFSR
KLAEIFMAFAIEDNYSKEEILELYVNTSYFGDGYYGIKEACNGYLDKEPSEMNLNECTMM
AGIPNAPSVYAPTKNPDLTKSRQEHVLETMVENGYISQEKAEEIINANT

Enzyme Prediction     

No EC number prediction in MGYG000001256_00960.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	41	211	2.9e-59	0.9661016949152542

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	4.53e-76	49	211	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	3.97e-72	49	226	4	181	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	2.42e-65	49	223	78	253	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	3.06e-63	49	226	69	246	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
COG4953	PbpC	5.81e-43	53	224	64	234	Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM09777.1	1.99e-82	3	225	19	241
QUO38940.1	1.11e-74	13	225	20	232
ADL05597.1	9.07e-68	23	224	10	211
QYX26381.1	1.98e-67	15	224	21	230
SET89048.1	6.69e-67	2	224	8	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3NB6_A	1.74e-40	49	226	22	199	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
2OQO_A	3.47e-40	49	226	22	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]
3UDF_A	8.36e-38	50	218	42	210	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	4.52e-37	50	228	42	224	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	1.70e-32	50	220	43	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
P38050	3.33e-41	2	221	6	241	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
Q07259	3.17e-39	30	218	30	217	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	3.63e-39	49	225	70	246	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA PE=3 SV=1
O87579	1.11e-37	49	226	70	247	Penicillin-binding protein 1A OS=Neisseria lactamica OX=486 GN=mrcA PE=3 SV=1
O86088	2.83e-37	49	226	70	247	Penicillin-binding protein 1A OS=Neisseria cinerea OX=483 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
0.799868	0.156610	0.034573	0.001332	0.000624	0.006993

TMHMM  Annotations     

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