Reviewed, UniProtKB/Swiss-Prot O59651 (KATG2_HALMA)

Names and origin

Protein names

Recommended name:
    Catalase-peroxidase 2
      Short name=CP 2
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase 2

Gene names

Name:	katG2
Synonyms:	Hmcp
Ordered Locus Names:	rrnAC1171

Organism

Haloarcula marismortui (Halobacterium marismortui) [Complete proteome] [HAMAP]

Taxonomic identifier

2238 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula

Protein attributes

Sequence length	731 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity.
Catalytic activity	2 H(2)O(2) = O(2) + 2 H(2)O. Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subunit structure	Homodimer.
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.
Mass spectrometry	Molecular weight is 81292±9 Da from positions 2 - 731. Determined by MALDI. Ref.1

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Complete proteome Direct protein sequencing
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: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron 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

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 731

730

Catalase-peroxidase 2

PRO_0000055580

Sites

Active site

96

1

Proton acceptor

Metal binding

259

1

Iron (heme axial ligand)

Site

92

1

Transition state stabilizer

Amino acid modifications

Cross-link

95 ↔ 218

Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244)

Cross-link

218 ↔ 244

Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-95)

Secondary structure

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731

Helix Strand Turn

Details...

Helix

23 – 26

4

Helix

34 – 37

4

Helix

52 – 58

7

Helix

61 – 72

12

Helix

82 – 84

3

Helix

87 – 98

12

Turn

103 – 105

3

Helix

114 – 116

3

Helix

120 – 122

3

Helix

124 – 126

3

Helix

129 – 135

7

Helix

137 – 143

7

Helix

144 – 146

3

Helix

149 – 163

15

Beta strand

217 – 219

3

Helix

224 – 226

3

Helix

230 – 242

13

Turn

243 – 245

3

Helix

248 – 258

11

Beta strand

266 – 268

3

Helix

270 – 273

4

Helix

278 – 280

3

Helix

283 – 285

3

Beta strand

303 – 306

4

Beta strand

309 – 314

6

Helix

321 – 328

8

Beta strand

331 – 335

5

Beta strand

341 – 348

8

Turn

349 – 352

4

Helix

370 – 377

8

Helix

379 – 390

12

Helix

392 – 408

17

Helix

414 – 416

3

Helix

428 – 430

3

Helix

443 – 455

13

Helix

460 – 471

12

Turn

476 – 479

4

Helix

487 – 489

3

Helix

493 – 495

3

Helix

497 – 499

3

Helix

501 – 521

21

Beta strand

524 – 526

3

Helix

530 – 548

19

Helix

566 – 568

3

Helix

571 – 574

4

Helix

575 – 577

3

Beta strand

580 – 582

3

Turn

583 – 586

4

Helix

596 – 606

11

Helix

611 – 624

14

Helix

628 – 630

3

Helix

646 – 652

7

Beta strand

656 – 660

5

Beta strand

665 – 672

8

Turn

673 – 675

3

Beta strand

678 – 683

6

Helix

684 – 687

4

Helix

688 – 690

3

Helix

693 – 702

10

Helix

708 – 724

17

Helix

728 – 730

3

Sequences

	Sequence		Length	Mass (Da)
	O59651-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0E12DE0CF72FF3A3	FASTA	731	81,384
	10 20 30 40 50 60 MAETPNSDMS GATGGRSKRP KSNQDWWPSK LNLEILDQNA RDVGPVEDDF DYAEEFQKLD 70 80 90 100 110 120 LEAVKSDLEE LMTSSQDWWP ADYGHYGPLF IRMAWHSAGT YRTADGRGGA AGGRQRFAPI 130 140 150 160 170 180 NSWPDNANLD KARRLLLPIK QKYGQKISWA DLMILAGNVA IESMGFKTFG YAGGREDAFE 190 200 210 220 230 240 EDKAVNWGPE DEFETQERFD EPGEIQEGLG ASVMGLIYVN PEGPDGNPDP EASAKNIRQT 250 260 270 280 290 300 FDRMAMNDKE TAALIAGGHT FGKVHGADDP EENLGPEPEA APIEQQGLGW QNKNGNSKGG 310 320 330 340 350 360 EMITSGIEGP WTQSPTEWDM GYINNLLDYE WEPEKGPGGA WQWAPKSEEL KNSVPDAHDP 370 380 390 400 410 420 DEKQTPMMLT TDIALKRDPD YREVMETFQE NPMEFGMNFA KAWYKLTHRD MGPPERFLGP 430 440 450 460 470 480 EVPDEEMIWQ DPLPDADYDL IGDEEIAELK EEILDSDLSV SQLVKTAWAS ASTYRDSDKR 490 500 510 520 530 540 GGANGARLRL EPQKNWEVNE PEQLETVLGT LENIQTEFND SRSDGTQVSL ADLIVLGGNA 550 560 570 580 590 600 AVEQAAANAG YDVEIPFEPG RVDAGPEHTD APSFDALKPK VDGVRNYIQD DITRPAEEVL 610 620 630 640 650 660 VDNADLLNLT ASELTALIGG MRSIGANYQD TDLGVFTDEP ETLTNDFFVN LLDMGTEWEP 670 680 690 700 710 720 AADSEHRYKG LDRDTGEVKW EATRIDLIFG SNDRLRAISE VYGSADAEKK LVHDFVDTWS 730 KVMKLDRFDL E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The protein sequence of an archaeal catalase-peroxidase." Cannac-Caffrey V., Hudry-Clergeon G., Petillot Y., Gagnon J., Zaccai G., Franzetti B. Biochimie 80:1003-1011(1998) [PubMed: 9924978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
[2]	"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea." Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V. Genome Res. 14:2221-2234(2004) [PubMed: 15520287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[3]	"The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui." Yamada Y., Fujiwara T., Sato T., Igarashi N., Tanaka N. Nat. Struct. Biol. 9:691-695(2002) [PubMed: 12172540] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-731.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y16851 Genomic DNA. Translation: CAA76423.1.
AY596297 Genomic DNA. Translation: AAV46121.1. Different initiation.

PIR

T44846.

RefSeq

YP_135827.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ITK	X-ray	2.00	A/B	1-731	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

2440. HmaCP01.

Genome annotation databases

GeneID

3129320.

GenomeReviews

Gene locus rrnAC1171 in contig AY596297_GR.

KEGG

hma:rrnAC1171.