dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

CAG-115 sp900768705

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; CAG-115; CAG-115 sp900768705

CAZyme ID

MGYG000003496_02067

CAZy Family

GT19

CAZyme Description

M18 family aminopeptidase 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
754		84140.67	7.8632

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003496	2237307	MAG	Fiji	Oceania

Gene Location

Start: 91; End: 2355 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000003496_02067.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT19	416	735	3.2e-98	0.903954802259887

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK02256	PRK02256	0.0	11	414	1	408	putative aminopeptidase 1; Provisional
cd05659	M18_API	0.0	30	414	2	394	M18 peptidase aminopeptidase I. Peptidase M18 family, aminopeptidase I (vacuolar aminopeptidase I; polypeptidase; Leucine aminopeptidase IV; LAPIV; aminopeptidase III; aminopeptidase yscI; EC 3.4.11.22) subfamily. Aminopeptidase I is widely distributed in bacteria and eukaryotes, but only the yeast enzyme has been characterized to date. It is a vacuolar enzyme, synthesized as a cytosolic proform, and proteolytically matured upon arrival in the vacuole. The pro-aminopeptidase I (proAPI) does not enter the vacuole via the secretory pathway. In non-starved cells, it uses the cytoplasm to vacuole targeting (cvt) pathway and in cells starved for nitrogen, it is targeted to the vacuole via autophagy. Yeast aminopeptidase I is active only in its dodecameric form with broad substrate specificity, acting on all aminoacyl and peptidyl derivatives that contain a free alpha-amino group; this is in contrast to the highly selective M18 mammalian aspartyl aminopeptidase. N-terminal leucine and most other hydrophobic amino acid residues are the best substrates while glycine and charged amino acid residues in P1 position are cleaved much more slowly. This enzyme is strongly and specifically activated by zinc (Zn2+) and chloride (Cl-) ions.
COG1362	LAP4	4.12e-117	26	414	1	382	Aspartyl aminopeptidase [Amino acid transport and metabolism].
cd05639	M18	1.28e-87	39	414	2	378	M18 peptidase aminopeptidase family. Peptidase M18 aminopeptidase family is widely distributed in bacteria and eukaryotes, but only the yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized to date. Yeast aminopeptidase I is active only in its dodecameric form with broad substrate specificity, acting on N-terminal leucine and most other amino acids. In contrast, the mammalian aspartyl aminopeptidase is highly selective for hydrolysis of N-terminal Asp or Glu residues from peptides. These enzymes have two catalytic zinc ions at the active site.
PRK00025	lpxB	1.99e-84	436	754	55	377	lipid-A-disaccharide synthase; Reviewed

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVJ81972.1	9.24e-147	418	752	36	365
ADE83537.1	2.93e-145	418	752	36	365
AVM56429.1	5.18e-144	418	754	36	378
QUB65076.1	2.63e-143	418	752	36	376
QKH89215.1	7.41e-143	418	752	36	376

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2GLJ_A	1.08e-137	15	419	1	413	crystalstructure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_B crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_C crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_D crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_E crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_F crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_G crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_H crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_I crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_J crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_K crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_L crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_M crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_N crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_O crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_P crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_Q crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_R crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_S crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_T crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_U crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_V crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_W crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum],2GLJ_X crystal structure of aminopeptidase I from Clostridium acetobutylicum [Clostridium acetobutylicum]
1Y7E_A	2.82e-120	17	431	1	422	ChainA, Probable M18-family aminopeptidase 1 [Borreliella burgdorferi]
2GLF_A	3.26e-112	18	419	3	401	Crystalstructure of Aminipeptidase (M18 family) from Thermotoga Maritima [Thermotoga maritima],2GLF_B Crystal structure of Aminipeptidase (M18 family) from Thermotoga Maritima [Thermotoga maritima],2GLF_C Crystal structure of Aminipeptidase (M18 family) from Thermotoga Maritima [Thermotoga maritima],2GLF_D Crystal structure of Aminipeptidase (M18 family) from Thermotoga Maritima [Thermotoga maritima]
5W8S_A	9.40e-22	466	735	90	365	LipidA Disaccharide Synthase (LpxB)-7 solubilizing mutations [Escherichia coli BL21(DE3)],5W8X_A Lipid A Disaccharide Synthase (LpxB)-7 solubilizing mutations-Bound to UDP [Escherichia coli BL21(DE3)]
5W8N_A	2.28e-21	466	735	90	365	LipidA Disaccharide Synthase (LpxB)-6 solubilizing mutations [Escherichia coli BL21(DE3)]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q97K30	6.74e-137	15	419	5	417	Probable M18 family aminopeptidase 1 OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=apeA PE=1 SV=1
Q661Q3	5.82e-123	17	419	1	410	Probable M18 family aminopeptidase 1 OS=Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 / PBi) OX=290434 GN=apeA PE=3 SV=1
Q0SNE8	5.82e-123	17	431	1	422	Probable M18 family aminopeptidase 1 OS=Borreliella afzelii (strain PKo) OX=390236 GN=apeA PE=3 SV=1
P0C925	2.79e-120	17	431	1	422	Probable M18 family aminopeptidase 1 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=apeA PE=1 SV=1
B7J1T9	2.79e-120	17	431	1	422	Probable M18 family aminopeptidase 1 OS=Borreliella burgdorferi (strain ZS7) OX=445985 GN=apeA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000052	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003496_02067.

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