CAZyme Information: MGYG000001626_01422

Basic Information

• Species: Phascolarctobacterium sp900544795
• Lineage: Bacteria; Firmicutes_C; Negativicutes; Acidaminococcales; Acidaminococcaceae; Phascolarctobacterium; Phascolarctobacterium sp900544795
• CAZyme ID: MGYG000001626_01422
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
277	MGYG000001626_9|CGC1	30292.64	4.8189

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001626	2152939	MAG	China	Asia

• Gene Location: Start: 47257; End: 48090 Strand: -

Full Sequence      

MFKIIIIIIAALGIFFWYPTSGNPVQEGPSPSDPQQQSLQHKNTETGKAAGFLLTLLPPK
QEWPDPAQKLWLAFNIEEAVNEHTSADTWVSITEIPLEMQQALLAIEDHNFYNHGAIDMD
GILRAALVNITAGEVVQGGSTITQQLTKNLFLSQEQTMSRKAEEAILALVLEHHYSKDQL
LEIYFNTTYFGAGATGIQAAAATYFNKAPNELQLAECAVIASLPYAPSALNPLENPEGCK
KRQRLVLQTMVKRGYIGTTMADKAAAEPLALANGLTL

Enzyme Prediction     

No EC number prediction in MGYG000001626_01422.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	84	251	1.3e-66	0.943502824858757

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00912	Transgly	1.01e-85	88	251	14	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	2.12e-84	88	271	3	186	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]
COG5009	MrcA	2.99e-76	90	269	70	249	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
COG0744	MrcB	3.57e-73	88	276	77	266	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
PRK11636	mrcA	8.09e-53	90	269	69	248	penicillin-binding protein 1a; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNP76977.1	4.13e-149	1	276	1	275
BBG64464.1	1.68e-148	1	276	1	275
QTV77901.1	3.06e-96	1	277	1	274
AVO26612.1	6.89e-64	59	271	45	262
ALG41193.1	6.89e-64	59	271	45	262

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2OQO_A	1.51e-51	63	264	4	197	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	6.04e-51	63	264	4	197	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
4OON_A	2.01e-41	88	269	40	221	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	1.94e-40	90	269	43	222	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]
3UDF_A	2.69e-40	90	271	42	223	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O66874	1.48e-48	51	269	18	245	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
Q07259	9.21e-46	78	271	38	230	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
P38050	2.18e-45	75	271	55	251	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O87626	4.87e-45	89	269	70	250	Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA PE=3 SV=1
O86088	2.91e-43	89	269	70	250	Penicillin-binding protein 1A OS=Neisseria cinerea OX=483 GN=mrcA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.322793	0.663183	0.012199	0.000692	0.000453	0.000670

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001626_01422.