CAZyme Information: MGYG000002478_00126

Basic Information

• Species: Phocaeicola dorei
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola dorei
• CAZyme ID: MGYG000002478_00126
• CAZy Family: GH28
• CAZyme Description: Putative non-heme bromoperoxidase BpoC

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
301	MGYG000002478_1|CGC7	34206.2	5.4297

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002478	5444912	Isolate	Finland	Europe

• Gene Location: Start: 179574; End: 180479 Strand: -

Full Sequence      

MNKNILIIICLLILSGLTGLYSQDTGDVQVKSGYVKVPEGSLYYEEAGTGEPLIFIHGHS
LDRRMWNEQFFKFAKHYRAIRYDLRGYGISSKQTEDFQFTHAEDLVALMDALHIRKAHIV
GLSLGGFVGADMLGCFPDRMLSAFLASGNIRKSKGPSEPMTKEEAAKRDEEIAALEKKGV
DVMKKEWFEGLMQSGGTRKERMRVPLWEMIDDWDAWQPLHKEVRVIIGLDAYAKLKENHP
QVPTLIVEGRSPGNRYSDHPEILDYLPNGKLKVLDDCGHMMNMEQPEAFNEALEEFLNDL
E

Enzyme Prediction     

No EC number prediction in MGYG000002478_00126.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0596	MhpC	4.56e-35	32	297	2	279	Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only].
TIGR02427	protocat_pcaD	1.99e-29	42	297	2	250	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]
pfam00561	Abhydrolase_1	6.28e-18	52	286	2	245	alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.
PRK14875	PRK14875	2.44e-16	24	297	103	368	acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
pfam12697	Abhydrolase_6	3.31e-15	53	292	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	8.02e-157	22	297	512	785
QUT92203.1	1.13e-156	22	297	512	785
QGX99118.1	1.24e-08	42	297	19	283
QIX26164.1	1.69e-07	61	296	45	291
QOZ51862.1	1.27e-06	42	145	19	127

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EGN_A	8.29e-22	42	297	11	260	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]
3FOB_A	1.87e-16	42	299	19	281	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]
3OM8_A	2.87e-16	41	297	16	264	Thecrystal structure of a hydrolase from Pseudomonas aeruginosa PA01 [Pseudomonas aeruginosa PAO1],3OM8_B The crystal structure of a hydrolase from Pseudomonas aeruginosa PA01 [Pseudomonas aeruginosa PAO1]
4UHH_A	8.23e-16	39	297	15	268	Structuralstudies of a thermophilic esterase from Thermogutta terrifontis (cacodylate complex) [Thermogutta terrifontis]
4UHC_A	9.09e-16	39	297	15	268	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O06734	5.13e-14	34	298	4	267	AB hydrolase superfamily protein YisY OS=Bacillus subtilis (strain 168) OX=224308 GN=yisY PE=3 SV=1
Q6F9F4	4.28e-13	41	297	13	259	(E)-2-((N-methylformamido)methylene)succinate hydrolase OS=Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) OX=62977 GN=tgnD PE=1 SV=1
P9WNH0	5.77e-13	41	296	3	256	Putative non-heme bromoperoxidase BpoC OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=bpoC PE=3 SV=1
P9WNH1	5.77e-13	41	296	3	256	Putative non-heme bromoperoxidase BpoC OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=bpoC PE=1 SV=1
P00632	8.34e-13	41	294	16	260	3-oxoadipate enol-lactonase 2 OS=Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) OX=62977 GN=catD PE=1 SV=3

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
0.001091	0.972478	0.025682	0.000261	0.000243	0.000220

TMHMM  Annotations     

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