C0ZDJ1 (C0ZDJ1_BREBN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Catalase-peroxidase HAMAP-Rule MF_01961
Short name=CP HAMAP-Rule MF_01961
EC=1.11.1.21 HAMAP-Rule MF_01961

Alternative name(s):
Peroxidase/catalase HAMAP-Rule MF_01961

Gene names

Name:	katG HAMAP-Rule MF_01961
Ordered Locus Names:	BBR47_28730

Organism

Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599) [Complete proteome] [HAMAP]

Taxonomic identifier

358681 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Brevibacillus › Brevibacillus brevis

Protein attributes

Sequence length	727 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity. HAMAP-Rule MF_01961
Catalytic activity	2 H2O2 = O2 + 2 H2O. HAMAP-Rule MF_01961 RuleBase RU003451 SAAS SAAS019793 Donor + H2O2 = oxidized donor + 2 H2O. HAMAP-Rule MF_01961 SAAS SAAS019793
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity. HAMAP-Rule MF_01961
Subunit structure	Homodimer or homotetramer By similarity. HAMAP-Rule MF_01961
Post-translational modification	The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP-Rule MF_01961
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily. HAMAP-Rule MF_01961 RuleBase RU003451

Ontologies

Keywords
Biological process	Hydrogen peroxide HAMAP-Rule MF_01961 RuleBase RU003451 SAAS SAAS019793
Ligand	Heme HAMAP-Rule MF_01961 RuleBase RU003900 SAAS SAAS000763 Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	catalase activity Inferred from electronic annotation. Source: HAMAP heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	102	1	Proton acceptor By similarity HAMAP-Rule MF_01961
	Metal binding	265	1	Iron (heme axial ligand) By similarity HAMAP-Rule MF_01961
	Site	98	1	Transition state stabilizer By similarity HAMAP-Rule MF_01961
Amino acid modifications
	Cross-link	101 ↔ 224		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with Met-250) By similarity HAMAP-Rule MF_01961
	Cross-link	224 ↔ 250		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-101) By similarity HAMAP-Rule MF_01961

Sequences

	Sequence		Length	Mass (Da)
	C0ZDJ1 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: 41AB15A04A9BEDD4	FASTA	727	80,061
	10 20 30 40 50 60 MDSMATANTG KCPFSHGSTT NHNPSATSNK HWWPNQLNLN ILHQHDRKSN PMGEEFDYAE 70 80 90 100 110 120 EFEKLDYQAL KQDLYDLMTN SQDWWPADYG HYGPLFIRMA WHSAGTYRTG DGRGGAGTGT 130 140 150 160 170 180 QRFAPLNSWP DNANLDKARR LLWPIKQKYG NKISWADLYI LAGNAAIESM GGKTIGFGGG 190 200 210 220 230 240 RADVWHPEED IYWGAEKEWL GDNRYTGDRD LENPLAAVQM GLIYVNPEGP NGNPDPLASA 250 260 270 280 290 300 RDIRETFKRM GMNDEETVAL VAGGHTFGKA HGAGDAALVG PEPEAAPLEA MGLGWQSTHG 310 320 330 340 350 360 SGKGRDAITS GIEGAWTANP TQWDNGFFEL LFGYEWELTK SPAGAHQWVA VNPADEHLAP 370 380 390 400 410 420 DAEDASVRVP TMMTTADMAL RMDPAYEKIS RRYYENPEEF ADAFATAWFK LTHRDMGPRS 430 440 450 460 470 480 RYLGPEVPEE DFIWQDPVPA AEYELTDADV AELKTRILDS GLTVSELVTT SWASASTFRG 490 500 510 520 530 540 SDMRGGSNGA RIRLAPQKEW EVNEPKKLEK VLTILGVIQE DFGKKVSMAD LIVLGGSAAV 550 560 570 580 590 600 EKAAQDAGFD VTVPFAPGRG DATQEQTDAE SFAVLEPIAD GFRNYQKKQY RVSPADLLID 610 620 630 640 650 660 KAQLLNLTAP EMTALVGGMR VIGTNHGGTQ HGVFTDRVGT LTNDFFVNLL DMGIQWKPVD 670 680 690 700 710 720 GGVFEGRDSK TGEVVRTATA VDLVFGSNSV LRAIAEVYAQ DDNKEKFVRD FIAAWVKVMN ADRFDLK

References

[1]

"Brevibacillus brevis strain 47, complete genome." Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W., Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S., Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H. , Udaka S., Tanikawa S., Fujita N. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 47 / JCM 6285 / NBRC 100599.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP008955 Genomic DNA. Translation: BAH43850.1.
RefSeq	YP_002772354.1. NC_012491.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	358681.BBR47_28730.
Protein family/group databases
PeroxiBase	7326. BbrCP01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAH43850; BAH43850; BBR47_28730.
GeneID	7715531.
KEGG	bbe:BBR47_28730.
PATRIC	21236086. VBIBreBre96763_2863.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0376.
HOGENOM	HOG000218110.
KO	K03782.
OMA	YRNWLKK.
ProtClustDB	PRK15061.
Enzyme and pathway databases
BioCyc	BBRE358681:GHYS-3001-MONOMER.
Family and domain databases
HAMAP	MF_01961. Catal_peroxid.
InterPro	IPR000763. Catalase_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 2 hits. [Graphical view]
PRINTS	PR00460. BPEROXIDASE. PR00458. PEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 2 hits.
TIGRFAMs	TIGR00198. cat_per_HPI. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C0ZDJ1_BREBN

Accession

Primary (citable) accession number: C0ZDJ1

Entry history

Integrated into UniProtKB/TrEMBL:	May 26, 2009
Last sequence update:	May 26, 2009
Last modified:	May 29, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)