KATG2_HALMA
ID KATG2_HALMA Reviewed; 731 AA.
AC O59651; Q5V2Y1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=Hmcp;
GN OrderedLocusNames=rrnAC1171;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND MASS
RP SPECTROMETRY.
RX PubMed=9924978; DOI=10.1016/s0300-9084(99)80005-4;
RA Cannac-Caffrey V., Hudry-Clergeon G., Petillot Y., Gagnon J., Zaccai G.,
RA Franzetti B.;
RT "The protein sequence of an archaeal catalase-peroxidase.";
RL Biochimie 80:1003-1011(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-731.
RX PubMed=12172540; DOI=10.1038/nsb834;
RA Yamada Y., Fujiwara T., Sato T., Igarashi N., Tanaka N.;
RT "The 2.0 A crystal structure of catalase-peroxidase from Haloarcula
RT marismortui.";
RL Nat. Struct. Biol. 9:691-695(2002).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01961};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- SUBUNIT: Homodimer.
CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC for the catalase, but not the peroxidase activity of the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- MASS SPECTROMETRY: Mass=81292; Mass_error=9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9924978};
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV46121.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y16851; CAA76423.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46121.1; ALT_INIT; Genomic_DNA.
DR PIR; T44846; T44846.
DR RefSeq; WP_049938864.1; NZ_CP039138.1.
DR PDB; 1ITK; X-ray; 2.00 A; A/B=1-731.
DR PDB; 3UW8; X-ray; 2.35 A; A/B=1-731.
DR PDB; 3VLH; X-ray; 1.73 A; A/B=1-731.
DR PDB; 3VLI; X-ray; 1.70 A; A/B=1-731.
DR PDB; 3VLJ; X-ray; 1.70 A; A/B=1-731.
DR PDB; 3VLK; X-ray; 2.00 A; A/B=1-731.
DR PDB; 3VLL; X-ray; 2.00 A; A/B=1-731.
DR PDB; 3VLM; X-ray; 2.33 A; A/B=1-731.
DR PDBsum; 1ITK; -.
DR PDBsum; 3UW8; -.
DR PDBsum; 3VLH; -.
DR PDBsum; 3VLI; -.
DR PDBsum; 3VLJ; -.
DR PDBsum; 3VLK; -.
DR PDBsum; 3VLL; -.
DR PDBsum; 3VLM; -.
DR AlphaFoldDB; O59651; -.
DR SMR; O59651; -.
DR STRING; 272569.rrnAC1171; -.
DR PeroxiBase; 2440; HmaCP01.
DR EnsemblBacteria; AAV46121; AAV46121; rrnAC1171.
DR GeneID; 40152166; -.
DR KEGG; hma:rrnAC1171; -.
DR PATRIC; fig|272569.17.peg.1887; -.
DR eggNOG; arCOG04487; Archaea.
DR HOGENOM; CLU_025424_2_0_2; -.
DR BRENDA; 1.11.1.21; 2549.
DR EvolutionaryTrace; O59651; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR HAMAP; MF_01961; Catal_peroxid; 1.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR30555; PTHR30555; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..731
FT /note="Catalase-peroxidase 2"
FT /id="PRO_0000055580"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT BINDING 259
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT SITE 92
FT /note="Transition state stabilizer"
FT CROSSLNK 95..218
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 244)"
FT CROSSLNK 218..244
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 95)"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:3VLI"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3VLH"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3VLJ"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:3VLI"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:3VLL"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:3VLL"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:3VLI"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:3VLI"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:3VLL"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1ITK"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 379..390
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 392..408
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 443..455
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 460..471
FT /evidence="ECO:0007829|PDB:3VLI"
FT TURN 476..479
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 501..521
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 530..548
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:3VLI"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 596..606
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 611..624
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 646..652
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 668..672
FT /evidence="ECO:0007829|PDB:3VLI"
FT TURN 673..675
FT /evidence="ECO:0007829|PDB:3VLI"
FT STRAND 678..682
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 684..687
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 688..690
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 693..702
FT /evidence="ECO:0007829|PDB:3VLI"
FT HELIX 708..723
FT /evidence="ECO:0007829|PDB:3VLI"
FT TURN 724..726
FT /evidence="ECO:0007829|PDB:3VLI"
FT TURN 728..730
FT /evidence="ECO:0007829|PDB:3VLH"
SQ SEQUENCE 731 AA; 81384 MW; 0E12DE0CF72FF3A3 CRC64;
MAETPNSDMS GATGGRSKRP KSNQDWWPSK LNLEILDQNA RDVGPVEDDF DYAEEFQKLD
LEAVKSDLEE LMTSSQDWWP ADYGHYGPLF IRMAWHSAGT YRTADGRGGA AGGRQRFAPI
NSWPDNANLD KARRLLLPIK QKYGQKISWA DLMILAGNVA IESMGFKTFG YAGGREDAFE
EDKAVNWGPE DEFETQERFD EPGEIQEGLG ASVMGLIYVN PEGPDGNPDP EASAKNIRQT
FDRMAMNDKE TAALIAGGHT FGKVHGADDP EENLGPEPEA APIEQQGLGW QNKNGNSKGG
EMITSGIEGP WTQSPTEWDM GYINNLLDYE WEPEKGPGGA WQWAPKSEEL KNSVPDAHDP
DEKQTPMMLT TDIALKRDPD YREVMETFQE NPMEFGMNFA KAWYKLTHRD MGPPERFLGP
EVPDEEMIWQ DPLPDADYDL IGDEEIAELK EEILDSDLSV SQLVKTAWAS ASTYRDSDKR
GGANGARLRL EPQKNWEVNE PEQLETVLGT LENIQTEFND SRSDGTQVSL ADLIVLGGNA
AVEQAAANAG YDVEIPFEPG RVDAGPEHTD APSFDALKPK VDGVRNYIQD DITRPAEEVL
VDNADLLNLT ASELTALIGG MRSIGANYQD TDLGVFTDEP ETLTNDFFVN LLDMGTEWEP
AADSEHRYKG LDRDTGEVKW EATRIDLIFG SNDRLRAISE VYGSADAEKK LVHDFVDTWS
KVMKLDRFDL E
