CAZyme Information: MGYG000002540_01609

Basic Information

• Species: Paraprevotella clara
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella clara
• CAZyme ID: MGYG000002540_01609
• CAZy Family: GH28
• CAZyme Description: Putative non-heme bromoperoxidase BpoC

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
298	MGYG000002540_22|CGC10	34267.37	6.6588

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002540	4187245	Isolate	not provided	not provided

• Gene Location: Start: 453470; End: 454366 Strand: -

Full Sequence      

MNSRKVWLWGCFCLIVGCMQARRPGEIRSAYVGVDHGTLYYEECGEGQPVILVHGHSLDH
RMWDGQFADLARDYRVIRYDLRGYGLSSPQTEDFQFTHVEDLVALMDSLHIEKAHVVGLS
LGGYIGADMLGWFPERMLSAFLASGNVRMSPGPSEPMDAEEAARRDREIAELKRKGVDVM
KREWFEGLMKSGGSRRERMRKPLWQMIQDWDAWQPLHKEVRVVAGKDAFRQLKTRKSDVP
VLIVEGKSPGNKFPEHPEILDYLPNGRMLVLEDCGHMMNMERPEEFNKALREFISKVE

Enzyme Prediction     

No EC number prediction in MGYG000002540_01609.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0596	MhpC	2.24e-37	28	297	1	282	Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only].
TIGR02427	protocat_pcaD	9.66e-34	38	295	1	251	3-oxoadipate enol-lactonase. Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]
PRK14875	PRK14875	2.57e-23	31	297	113	371	acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
pfam00561	Abhydrolase_1	5.46e-22	49	283	2	245	alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.
pfam12697	Abhydrolase_6	1.30e-15	50	289	1	212	Alpha/beta hydrolase family. This family contains alpha/beta hydrolase enzymes of diverse specificity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALJ62047.1	1.69e-143	20	296	508	787
QUT92203.1	2.38e-143	20	296	508	787
QIX26164.1	2.58e-11	20	293	7	291
QGX99118.1	4.62e-11	19	296	1	285
CAE5966245.1	1.30e-08	46	298	608	908

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EGN_A	5.77e-23	31	295	3	261	Est816as an N-Acyl homoserine lactone degrading enzyme [uncultured bacterium],5EGN_B Est816 as an N-Acyl homoserine lactone degrading enzyme [uncultured bacterium],5EGN_C Est816 as an N-Acyl homoserine lactone degrading enzyme [uncultured bacterium],5EGN_D Est816 as an N-Acyl homoserine lactone degrading enzyme [uncultured bacterium],5EGN_E Est816 as an N-Acyl homoserine lactone degrading enzyme [uncultured bacterium],5EGN_F Est816 as an N-Acyl homoserine lactone degrading enzyme [uncultured bacterium],5EGN_G Est816 as an N-Acyl homoserine lactone degrading enzyme [uncultured bacterium],5EGN_H Est816 as an N-Acyl homoserine lactone degrading enzyme [uncultured bacterium]
4UHH_A	5.79e-21	24	297	13	271	Structuralstudies of a thermophilic esterase from Thermogutta terrifontis (cacodylate complex) [Thermogutta terrifontis]
4UHC_A	6.60e-21	24	297	13	271	Structuralstudies of a thermophilic esterase from Thermogutta terrifontis (Native) [Thermogutta terrifontis],4UHD_A Structural studies of a thermophilic esterase from Thermogutta terrifontis (acetate bound) [Thermogutta terrifontis],4UHE_A Structural studies of a thermophilic esterase from Thermogutta terrifontis (malate bound) [Thermogutta terrifontis],4UHF_A Structural studies of a thermophilic esterase from Thermogutta terrifontis (L37A mutant with butyrate bound) [Thermogutta terrifontis]
3FOB_A	1.63e-19	39	294	19	279	Crystalstructure of bromoperoxidase from Bacillus anthracis [Bacillus anthracis str. Ames],3FOB_B Crystal structure of bromoperoxidase from Bacillus anthracis [Bacillus anthracis str. Ames],3FOB_C Crystal structure of bromoperoxidase from Bacillus anthracis [Bacillus anthracis str. Ames]
7LD8_A	1.79e-18	38	297	11	268	ChainA, Putative non-heme bromoperoxidase BpoC [Mycobacterium tuberculosis H37Rv]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P9WNH1	5.92e-17	38	297	3	260	Putative non-heme bromoperoxidase BpoC OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=bpoC PE=1 SV=1
P9WNH0	5.92e-17	38	297	3	260	Putative non-heme bromoperoxidase BpoC OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=bpoC PE=3 SV=1
O06734	8.23e-16	35	293	9	265	AB hydrolase superfamily protein YisY OS=Bacillus subtilis (strain 168) OX=224308 GN=yisY PE=3 SV=1
Q59695	1.65e-15	17	296	104	369	Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system OS=Pseudomonas putida OX=303 GN=acoC PE=3 SV=1
O31168	8.51e-15	32	144	6	125	Non-heme chloroperoxidase OS=Kitasatospora aureofaciens OX=1894 GN=cpo PE=1 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
0.000897	0.859284	0.138883	0.000423	0.000270	0.000216

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002540_01609.