Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Vegetative catalase

Gene

katA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

heme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541PROSITE-ProRule annotation
Active sitei127 – 1271PROSITE-ProRule annotation
Metal bindingi337 – 3371Iron (heme axial ligand)By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU08820-MONOMER.

Protein family/group databases

PeroxiBasei4082. BsKat01_168.

Names & Taxonomyi

Protein namesi
Recommended name:
Vegetative catalase (EC:1.11.1.6)
Gene namesi
Name:katA
Synonyms:kat, kat-19
Ordered Locus Names:BSU08820
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 483482Vegetative catalasePRO_0000084975Add
BLAST

Proteomic databases

PaxDbiP26901.

Expressioni

Developmental stagei

Elevated levels of expression during entry into the stationary phase of the growth cycle.

Inductioni

By hydrogen peroxide.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004888.

Structurei

3D structure databases

ProteinModelPortaliP26901.
SMRiP26901. Positions 6-475.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiCOG0753. LUCA.
HOGENOMiHOG000087852.
InParanoidiP26901.
KOiK03781.
OMAiRYNHREG.
OrthoDBiEOG6P5Z9F.
PhylomeDBiP26901.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSNKLTTSW GAPVGDNQNS MTAGSRGPTL IQDVHLLEKL AHFNRERVPE
60 70 80 90 100
RVVHAKGAGA HGYFEVTNDV TKYTKAAFLS EVGKRTPLFI RFSTVAGELG
110 120 130 140 150
SADTVRDPRG FAVKFYTEEG NYDIVGNNTP VFFIRDAIKF PDFIHTQKRD
160 170 180 190 200
PKTHLKNPTA VWDFWSLSPE SLHQVTILMS DRGIPATLRH MHGFGSHTFK
210 220 230 240 250
WTNAEGEGVW IKYHFKTEQG VKNLDVNTAA KIAGENPDYH TEDLFNAIEN
260 270 280 290 300
GDYPAWKLYV QIMPLEDANT YRFDPFDVTK VWSQKDYPLI EVGRMVLDRN
310 320 330 340 350
PENYFAEVEQ ATFSPGTLVP GIDVSPDKML QGRLFAYHDA HRYRVGANHQ
360 370 380 390 400
ALPINRARNK VNNYQRDGQM RFDDNGGGSV YYEPNSFGGP KESPEDKQAA
410 420 430 440 450
YPVQGIADSV SYDHYDHYTQ AGDLYRLMSE DERTRLVENI VNAMKPVEKE
460 470 480
EIKLRQIEHF YKADPEYGKR VAEGLGLPIK KDS
Length:483
Mass (Da):54,791
Last modified:June 16, 2009 - v5
Checksum:i63BC1F23B6A39E16
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061G → P in AAA22402 (PubMed:1756979).Curated
Sequence conflicti373 – 3731D → G in CAB04807 (PubMed:9202460).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80796 Genomic DNA. Translation: AAA22402.1.
Z82044 Genomic DNA. Translation: CAB04807.1.
AL009126 Genomic DNA. Translation: CAB12710.2.
PIRiJH0532.
RefSeqiNP_388762.2. NC_000964.3.
WP_003245322.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB12710; CAB12710; BSU08820.
GeneIDi939240.
KEGGibsu:BSU08820.
PATRICi18973456. VBIBacSub10457_0923.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80796 Genomic DNA. Translation: AAA22402.1.
Z82044 Genomic DNA. Translation: CAB04807.1.
AL009126 Genomic DNA. Translation: CAB12710.2.
PIRiJH0532.
RefSeqiNP_388762.2. NC_000964.3.
WP_003245322.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliP26901.
SMRiP26901. Positions 6-475.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004888.

Protein family/group databases

PeroxiBasei4082. BsKat01_168.

Proteomic databases

PaxDbiP26901.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12710; CAB12710; BSU08820.
GeneIDi939240.
KEGGibsu:BSU08820.
PATRICi18973456. VBIBacSub10457_0923.

Phylogenomic databases

eggNOGiCOG0753. LUCA.
HOGENOMiHOG000087852.
InParanoidiP26901.
KOiK03781.
OMAiRYNHREG.
OrthoDBiEOG6P5Z9F.
PhylomeDBiP26901.

Enzyme and pathway databases

BioCyciBSUB:BSU08820-MONOMER.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The isolation, cloning and identification of a vegetative catalase gene from Bacillus subtilis."
    Bol D.K., Yasbin R.E.
    Gene 109:31-37(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / YB886 / BG214.
  2. "The Bacillus subtilis 168 chromosome from sspE to katA."
    Cummings N.J., Connerton I.F.
    Microbiology 143:1855-1859(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 373.
  5. "Isolation and characterization of a hydrogen peroxide resistant mutant of Bacillus subtilis."
    Hartford O.M., Dowds B.C.A.
    Microbiology 140:297-304(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19.
    Strain: 168 / YB886 / BG214.
  6. "Proteome analysis of Bacillus subtilis extracellular proteins: a two-dimensional protein electrophoretic study."
    Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.
    Microbiology 146:65-75(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: 168.
  7. Bano S., Qader S.A.U., Aman A., Azhar A.
    Submitted (AUG-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: KIBGE-HAS.
  8. "The frataxin homologue Fra plays a key role in intracellular iron channeling in Bacillus subtilis."
    Albrecht A.G., Landmann H., Nette D., Burghaus O., Peuckert F., Seubert A., Miethke M., Marahiel M.A.
    ChemBioChem 12:2052-2061(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IRON-BINDING, COFACTOR, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: ATCC 21332 / IAM 1213.

Entry informationi

Entry nameiCATA_BACSU
AccessioniPrimary (citable) accession number: P26901
Secondary accession number(s): P77838
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 16, 2009
Last modified: July 6, 2016
This is version 124 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.