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   08-NOV-2023, entry version 140.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PaxDb; 272569-rrnAC1171; -.
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   CDD; cd00649; catalase_peroxidase_1; 1.
DR   CDD; cd08200; catalase_peroxidase_2; 1.
DR   Gene3D; 1.10.520.10; -; 2.
DR   Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
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   NCBIfam; TIGR00198; cat_per_HPI; 1.
DR   PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR   PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
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
//