dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001787_00487

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Basic Information help

Species

Phocaeicola sp900551645

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900551645

CAZyme ID

MGYG000001787_00487

CAZy Family

GH33

CAZyme Description

Hercynine oxygenase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
643	MGYG000001787_8\|CGC2	71740.77	6.4184

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001787	3320861	MAG	Denmark	Europe

Gene Location

Start: 53001; End: 54932 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001787_00487.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH33	288	587	8.8e-25	0.8333333333333334

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1262	YfmG	4.15e-54	29	250	52	310	Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones].
pfam03781	FGE-sulfatase	1.21e-52	29	250	4	258	Sulfatase-modifying factor enzyme 1. This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.
cd15482	Sialidase_non-viral	3.07e-39	283	587	11	304	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
pfam13088	BNR_2	1.55e-23	297	585	1	260	BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
COG4692	COG4692	0.001	263	639	12	377	Predicted neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
ADV43483.1	15	639	12	642
QGT74043.1	24	640	22	663
SCV08950.1	22	640	16	663
ALJ49526.1	22	640	16	663
QRQ56304.1	22	640	16	663

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5HHA_A	2.43e-28	21	251	33	284	Structureof PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5HHA_B Structure of PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]
1Y1F_X	2.30e-23	29	261	18	303	humanformylglycine generating enzyme with cysteine sulfenic acid [Homo sapiens],1Y1J_X human formylglycine generating enzyme, sulfonic acid/desulfurated form [Homo sapiens]
1Y1E_X	2.30e-23	29	261	18	303	humanformylglycine generating enzyme [Homo sapiens],1Y1H_X human formylglycine generating enzyme, oxidised Cys refined as hydroperoxide [Homo sapiens],1Y1I_X hyuman formylglycine generating enzyme, reduced form [Homo sapiens]
1Y1G_X	2.30e-23	29	261	18	303	Humanformylglycine generating enzyme, double sulfonic acid form [Homo sapiens],1Z70_X 1.15A resolution structure of the formylglycine generating enzyme FGE [Homo sapiens]
6MUJ_A	2.64e-23	31	248	32	305	Formylglycinegenerating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_B Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_C Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_D Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_E Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9F3C7	1.33e-22	31	248	27	300	Formylglycine-generating enzyme OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=SCO7548 PE=1 SV=1
Q7AJA5	2.01e-22	27	252	382	617	Serine/threonine-protein kinase pkn1 OS=Chlamydia pneumoniae OX=83558 GN=pkn1 PE=3 SV=1
Q8R0F3	4.34e-22	26	254	85	368	Formylglycine-generating enzyme OS=Mus musculus OX=10090 GN=Sumf1 PE=1 SV=2
Q8NBK3	1.09e-21	29	254	90	370	Formylglycine-generating enzyme OS=Homo sapiens OX=9606 GN=SUMF1 PE=1 SV=3
Q0P5L5	2.64e-21	29	254	90	370	Formylglycine-generating enzyme OS=Bos taurus OX=9913 GN=SUMF1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000453	0.998768	0.000273	0.000169	0.000164	0.000151

TMHMM Annotations help

There is no transmembrane helices in MGYG000001787_00487.