CAZyme Information: MGYG000004824_00276

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella
• CAZyme ID: MGYG000004824_00276
• CAZy Family: GH28
• CAZyme Description: Putative non-heme bromoperoxidase BpoC

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
304	MGYG000004824_2|CGC1	34881.79	5.7863

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004824	2984736	MAG	China	Asia

• Gene Location: Start: 30879; End: 31793 Strand: +

Full Sequence      

MKLKLRRVVFLVCLLVTAYVRGEGADSVKTAYIPVEKGTLYYEECGHGSPVILVHGHSLD
HRMWNDQFYELSQRHRVIRYDLRGYGRSSSQIEGFQFTHVEDLVALMDSLHISKAHVVGL
SLGGYVGADMLGWFPERMLSAFLASGNVRMSKGPSEPMTDEESRQRDREIAELKQRGVDV
MKKEWFEGLMNSGGSQRERMRESLWQMIDDWDAWQPLHKEARVVAGKDAFEKLKINRPDV
PVMVVEGRSEGNRFPEHPEILDYLPNGQIQILDDCGHMMNMERPEEFNVLLNAFLDRIDA
EIGQ

Enzyme Prediction     

No EC number prediction in MGYG000004824_00276.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0596	MhpC	3.52e-32	30	298	2	282	Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only].
TIGR02427	protocat_pcaD	1.61e-28	39	296	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]
pfam00561	Abhydrolase_1	6.08e-20	50	284	2	245	alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.
PRK14875	PRK14875	4.85e-19	15	295	89	368	acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
pfam12697	Abhydrolase_6	1.93e-14	51	288	1	210	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
QUT92203.1	3.77e-138	20	295	511	785
ALJ62047.1	5.33e-138	20	295	511	785
QIX26164.1	2.25e-09	48	296	33	293
QGX99118.1	4.01e-09	40	297	19	285
QMU58029.1	3.09e-07	40	295	19	280

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EGN_A	1.68e-21	40	295	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]
4UHC_A	1.71e-18	40	303	18	276	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]
4UHH_A	1.03e-17	40	301	18	274	Structuralstudies of a thermophilic esterase from Thermogutta terrifontis (cacodylate complex) [Thermogutta terrifontis]
3FOB_A	2.14e-17	34	295	16	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]
1HKH_A	2.81e-14	34	145	12	124	unligatedgamma lactamase from an Aureobacterium species [Microbacterium],1HKH_B unligated gamma lactamase from an Aureobacterium species [Microbacterium],1HL7_A Gamma lactamase from an Aureobacterium species in complex with 3a,4,7,7a-tetrahydro-benzo [1,3] dioxol-2-one [Microbacterium sp.],1HL7_B Gamma lactamase from an Aureobacterium species in complex with 3a,4,7,7a-tetrahydro-benzo [1,3] dioxol-2-one [Microbacterium sp.]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O06734	3.90e-14	32	294	4	265	AB hydrolase superfamily protein YisY OS=Bacillus subtilis (strain 168) OX=224308 GN=yisY PE=3 SV=1
P27747	5.21e-14	22	295	108	372	Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system OS=Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) OX=381666 GN=acoC PE=1 SV=3
P9WNH1	4.38e-13	40	300	4	262	Putative non-heme bromoperoxidase BpoC OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=bpoC PE=1 SV=1
P9WNH0	4.38e-13	40	300	4	262	Putative non-heme bromoperoxidase BpoC OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=bpoC PE=3 SV=1
A8IAD8	4.54e-13	40	299	11	264	Putative carbamate hydrolase RutD OS=Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB 13405 / ORS 571) OX=438753 GN=rutD 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
0.000211	0.999173	0.000172	0.000153	0.000141	0.000131

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004824_00276.