CAZyme Information: MGYG000001388_04526

Basic Information

• Species: Desulfitobacterium hafniense
• Lineage: Bacteria; Firmicutes_B; Desulfitobacteriia; Desulfitobacteriales; Desulfitobacteriaceae; Desulfitobacterium; Desulfitobacterium hafniense
• CAZyme ID: MGYG000001388_04526
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
229	MGYG000001388_60|CGC3	26642.26	4.9853

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001388	5194328	Isolate	not provided	not provided

• Gene Location: Start: 388001; End: 388690 Strand: +

Full Sequence      

MDYTRYVVQPGDSIYKIANAYKIEMSDIINLNHLKHPDRIYPGQILLLPTYEFKDTLPGE
IPEPNFTYAMWLFDVYAGKDSELSAVTTYLYQAVVLDRPEFDELLRPIAYDELRHLEQLA
WCIRFLGVDPRYGSFSKGRWFDWRSRYLNYSTELCVILDHNMKDEAAAVKHYTDLAQKIP
IPEIQTILLQLAADEERHYQCLAQAKTRFCGCGSSQTQHIKESSNGEEL

Enzyme Prediction     

No EC number prediction in MGYG000001388_04526.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07908	Mn_catalase_like	3.12e-30	58	202	4	150	Manganese catalase-like protein, ferritin-like diiron-binding domain. This uncharacterized bacterial protein family has a ferritin-like domain similar to that of the manganese catalase protein of Lactobacillus plantarum and the bll3758 protein of Bradyrhizobium japonicum. Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).
pfam01476	LysM	9.52e-15	6	49	1	43	LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
cd00118	LysM	1.30e-13	4	48	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
smart00257	LysM	2.18e-13	6	48	2	44	Lysin motif.
cd00657	Ferritin_like	1.09e-12	71	199	2	123	Ferritin-like superfamily of diiron-containing four-helix-bundle proteins. Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAE84981.1	4.35e-173	1	229	1	229
CDX03304.1	7.22e-172	1	229	1	229
AGA70483.1	4.95e-147	1	228	1	228
AHF07942.1	5.87e-129	1	211	1	211
AFQ46039.1	8.41e-103	1	210	1	214

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001388_04526.