A0LZM9 (KATG_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase-peroxidase
Short name=CP
EC=1.11.1.21

Alternative name(s):
Peroxidase/catalase

Gene names

Name:	katG
Ordered Locus Names:	GFO_0850

Organism

Gramella forsetii (strain KT0803) [Complete proteome] [HAMAP]

Taxonomic identifier

411154 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Gramella

Protein attributes

Sequence length	750 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 MF_01961
Catalytic activity	Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961 2 H2O2 = O2 + 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. HAMAP 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 MF_01961
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
Molecular function	catalase activity Inferred from electronic annotation. Source: InterPro 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 – 750	750	Catalase-peroxidase HAMAP MF_01961		PRO_0000354804
Sites
	Active site	113	1	Proton acceptor By similarity
	Metal binding	276	1	Iron (heme axial ligand) By similarity
	Site	109	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	112 ↔ 235		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-261) By similarity
	Cross-link	235 ↔ 261		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-112) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0LZM9 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 5D1FB60D78C142B9	FASTA	750	83,111
	10 20 30 40 50 60 MGNNKSGSED NHKVWEVNES SKCPFMGGAL NKTAGKGTSN RDWWPNQLNL NILRQNSSLI 70 80 90 100 110 120 NPMDDGFNYA EAFKSLDLNA VKQDIYDLMT NSQDWWPADY GHYGPFFIRM AWHSAGTYRI 130 140 150 160 170 180 GDGRGGAGSG QQRFAPLNSW PDNANLDKAR LLLWPVKKKY GKNLSWADLL VLAGNCAHES 190 200 210 220 230 240 MGLKMFGFAG GREDVWEPAQ DVYWGAETEW LNNDERYAGE ELENPLGAAH MGLIYVNPEG 250 260 270 280 290 300 HNGNPDPVEA ASYIRETFGR MAMNDYETVA LIAGGHTFGK THGAADAEEY VEAEPAAAGI 310 320 330 340 350 360 ESQGLGWKNT FGTGNGADTI TSGIEGAWTD TPTKWSNKYF DNLFKYDWEC IKGPGGAYQW 370 380 390 400 410 420 QPKDNAGAGT VPDAHDPDKK HAPFMLTTDL SLKMDPEYEK ISRHFYENPD EFADAYSRAW 430 440 450 460 470 480 FKLTHRDMGP IERYLGPEVP KEELLWQDPI PKVDHEIIND SDIASLKNKI LNTGLSVQEL 490 500 510 520 530 540 VTTAWGSAST FRGSDKRGGA NGGRIRLAPQ NGWEVNNPKQ LGKVIDTLEK IQQDFNESQS 550 560 570 580 590 600 GSKKVSIADL IVLAGCVGVE KAAKTAGHEL KVPFSPGRAD ASQEQTDVEA FEPLEPNADG 610 620 630 640 650 660 FRNYFRNRDH VSASAEELLV DRAQLLTLTV PQMTVLLGGM RAMGANYDGS KKGVFTDRPG 670 680 690 700 710 720 QLTNDFFKNI LEMGLTWKSS SDSETEFDGS DRKTGDVKWT GSRADLIFGS NSELRAIAEV 730 740 750 YGTDDVEAKF VKDFVKAWDK VMNLDRYDLK

References

[1]

"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter." Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O. Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KT0803.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU207366 Genomic DNA. Translation: CAL65824.1.
RefSeq	YP_860891.1. NC_008571.1.
3D structure databases
ProteinModelPortal	A0LZM9.
SMR	A0LZM9. Positions 37-749.
ModBase	Search...
Protein-protein interaction databases
STRING	A0LZM9.
Protein family/group databases
PeroxiBase	6253. GfoCP01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4652021.
GenomeReviews	Gene locus GFO_0850 in contig CU207366_GR.
KEGG	gfo:GFO_0850.
NMPDR	fig|411154.5.peg.811.
PATRIC	22070551. VBIGraFor5527_0822.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0376.
HOGENOM	HBG285610.
OMA	KRHAPSM.
PhylomeDB	A0LZM9.
ProtClustDB	PRK15061.
Enzyme and pathway databases
BioCyc	GFOR411154:GFO_0850-MONOMER.
Family and domain databases
HAMAP	MF_01961. Catal-peroxid. [Tree]
InterPro	IPR000763. Catalase_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
KO	K03782.
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

KATG_GRAFK

Accession

Primary (citable) accession number: A0LZM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	December 12, 2006
Last modified:	December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program