Q2RZX7 (KATG_SALRD) 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:	SRU_2405

Organism

Salinibacter ruber (strain DSM 13855 / M31)

Taxonomic identifier

309807 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidetes Order II. Incertae sedis › Rhodothermaceae › Salinibacter

Protein attributes

Sequence length	729 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 Reference 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 – 729	729	Catalase-peroxidase HAMAP MF_01961		PRO_0000354901
Sites
	Active site	92	1	Proton acceptor By similarity
	Metal binding	255	1	Iron (heme axial ligand) By similarity
	Site	88	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	91 ↔ 214		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-240) By similarity
	Cross-link	214 ↔ 240		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2RZX7 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 4D127EFC5C88E187	FASTA	729	82,038
	10 20 30 40 50 60 MHNGSNGSVE QRDSMPETSR EWWPGSLDVE ILDQNAQDVG PWNGDFDYAE AFQELDYEAL 70 80 90 100 110 120 KEDIEEVMTT SKDWWPADYG HYGPLFIRMS WHAAGTYRTT DGRGGSSGGR QRLAPLNSWP 130 140 150 160 170 180 DNANLDKARR LLWPVKQKYG RKISWADLLV LAGNVAMESM GFETFGFAGG REDDFKPDES 190 200 210 220 230 240 IDWGPEDEME TWGRFNEEDE LDNPLGATVM GLIYVNPEGP ESTPDPEWSA QRIRKSFGRM 250 260 270 280 290 300 AMNDRETAAL IAGGHTFGKV HGADTDEHLQ AEPEAAPIEQ QGLGWHNEHG SGKGGDTITS 310 320 330 340 350 360 GIEGPWTDAP TEWDMGYLDF LLDYEWEVHK GPGGAWQWRP KSDELKGVVP DAHDASETVD 370 380 390 400 410 420 PMMLTTDVAL KRDPDYREII EDFRENPDAF EDAFARAWFK LLHRDMGPKE RYLGPEVPEE 430 440 450 460 470 480 DLIWQDPVPD ADHDLIGDEE IAELKEAILE TDLSVSRLVK TAWASASTYR DSDKRGGANG 490 500 510 520 530 540 ARIRLEPHRN WEANEPPQLA HALEVLTGIQ KNFNDARTDD VRVSLADLIV LGGSAAIEKA 550 560 570 580 590 600 AADAGHDVEV PFTPGRTDAT QEQTDVEAFE YLEPKADGFR NYIADDPWQD WTPEEFLVDK 610 620 630 640 650 660 ADLLNLTPAE TTVLVGGMRA LDATHEQADG YGVFTDRPET LNNDYFVNLL DMGHEWDPVS 670 680 690 700 710 720 EDKQHFKIRD RDTGEVKWKA TRVDLIFGSN SRFRALSQVY GSGDAEEKFV DDFVDAWTKV MNLDRFDLE

References

[1]

"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea." Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F. Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed: 16330755] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13855 / M31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000159 Genomic DNA. Translation: ABC45695.1.
RefSeq	YP_446504.1. NC_007677.1.
3D structure databases
HSSP	HSSP built from PDB template 1U2L based on UniProtKB P13029.
ProteinModelPortal	Q2RZX7.
SMR	Q2RZX7. Positions 16-729.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2RZX7.
Protein family/group databases
PeroxiBase	3063. SruCP01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3851567.
GenomeReviews	Gene locus SRU_2405 in contig CP000159_GR.
KEGG	sru:SRU_2405.
NMPDR	fig|309807.5.peg.2275.
PATRIC	23427373. VBISalRub86502_2505.
TIGR	SRU_2405.
Phylogenomic databases
eggNOG	COG0376.
HOGENOM	HBG285610.
OMA	KRHAPSM.
PhylomeDB	Q2RZX7.
ProtClustDB	PRK15061.
Enzyme and pathway databases
BioCyc	SRUB309807:SRU_2405-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_SALRD

Accession

Primary (citable) accession number: Q2RZX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program