Reviewed, UniProtKB/Swiss-Prot Q1IRZ2 (KATG_ACIBL)

Names and origin

Protein names

Recommended name:
    Catalase-peroxidase
      Short name=CP
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase

Gene names

Name:	katG
Ordered Locus Names:	Acid345_1356

Organism

Acidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Candidatus Koribacter

Protein attributes

Sequence length	752 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

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

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme 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 oxidation reduction 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 752	752	Catalase-peroxidase HAMAP MF_01961		PRO_0000354709
Sites
	Active site	112	1	Proton acceptor By similarity
	Metal binding	275	1	Iron (heme axial ligand) By similarity
	Site	108	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	111 ↔ 234		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-260) By similarity
	Cross-link	234 ↔ 260		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-111) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1IRZ2-1 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: A34B0B095FBDC49E	FASTA	752	82,957
	10 20 30 40 50 60 MENELVSKVK APVPGNQTNT LNEAKCPVGA HTLAGARSNA NWWPNQLNIN ILHQHSPLSD 70 80 90 100 110 120 PMPEGFNYAE EFKTLDLDAV VKDLRHLMTD SQPWWPADYG HYGPFFIRMA WHSAGTYRIG 130 140 150 160 170 180 DGRGGAGSGE QRFAPLNSWP DNGNLDKARR LLWPIKQKYG RKLSWADLMV LAGNVALESM 190 200 210 220 230 240 GFKTFGFAGG REDVWEPSED IYWGPEGKWL DDKRYSGERD LENPLGAVQM GLIYVNPEGP 250 260 270 280 290 300 NGKPDPAAAA VDIRETFARM AMNDEETVAL IAGGHTFGKT HGAGVPTEYV GPEPEGAGIE 310 320 330 340 350 360 EQGLGWKNKL GHGHGYHTIT SGLEGAWTTN PIKWDNGFFD NLFGYDWELT KSPAGANQWT 370 380 390 400 410 420 PKNGAGKDTV PDAHDKTKRH APFMATTDIS LKVDPIYGPI SKRFHEHPQE FADAFAKAWY 430 440 450 460 470 480 KLTHRDMGPL PRYLGKLVPK EPQVWQDPVP AVDHELVNDS DVAALKAKLL ASGLTVSQLV 490 500 510 520 530 540 TTAWAAASSF RGSDKRGGAN GARIRLTPQK DWEVNQPKEL AKVLPVLEKI QHDFNAQGGK 550 560 570 580 590 600 KKISLADLII LGGCAAVEEA AKKGGHSVKV PFTPGRTDAS QEHTDVKSFS VMEPKADGFR 610 620 630 640 650 660 NYHQKGQPRP AEEMLVDKAQ LLRLTAPEMT ALVGGLRVLG ANYGHSKHGV FTSHPETLTN 670 680 690 700 710 720 DFFVNLLDMN NRWQPSGADG VYEARDRQGD HVKWTATRVD LIFGSHSQLR AFAEVYACND 730 740 750 AKEKFVHDFV AAWTKVMNLD RYDLAKKKAA AN

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000360 Genomic DNA. Translation: ABF40358.1.
RefSeq	YP_590432.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IRZ2.
Genome annotation databases
GeneID	4070894.
GenomeReviews	Gene locus Acid345_1356 in contig CP000360_GR.
KEGG	aba:Acid345_1356.
NMPDR	fig|204669.6.peg.1342.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1IRZ2.
OMA	FEWELTK.
Family and domain databases
HAMAP	MF_01961. [Tree]
InterPro	IPR000763. Catalase_proxase. 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.
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

KATG_ACIBL

Accession

Primary (citable) accession number: Q1IRZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	June 13, 2006
Last modified:	November 3, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)