CAZyme Information: MGYG000001639_00509

Basic Information

• Species: Haloferax massiliensis
• Lineage: Archaea; Halobacteriota; Halobacteria; Halobacteriales; Haloferacaceae; Haloferax; Haloferax massiliensis
• CAZyme ID: MGYG000001639_00509
• CAZy Family: AA2
• CAZyme Description: Catalase-peroxidase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
718		79890.35	3.9094

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001639	3991467	Isolate	not provided	not provided

• Gene Location: Start: 523992; End: 526148 Strand: -

Full Sequence      

MNGSDHDWWPDQLDLEILDQNAQQIDPMGEEFDYAEEFQNLDYDQLKADIEEVLTDSKDW
WPADYGHYGPLFIRMAWHSAGTYRAHDGRGGASGGHQRLPPISSWPDNVNLDKARRLLWP
VKKKYGNQLSWGDLIVLAGNVALESMGFETFGFAGGRADDYVGDKAPSWGPEEEWETTSA
ERFDEEGNLKEPLGNTVMGLIYVNPEGPNGEPDLEGSAKNIRETFSGMAMNDKETVALIA
GGHTFGKVHGADSGDNLEAEPEAAPIEEQGLGWKNNHGSGKGPDTITSGIEGPWTSAPTQ
WDMGYVANLLDYEWEAHKGPGGAWQWRPADESPADKIPDAAPDAHLPDQFVDPMMLTTDI
ALKKDPDFRAVLEEFREDPAEFQESFAKAWYKLLHRDMGPPSRLVGPEVPDEAMLWQDPI
PDADYDLIDDEDVEELKAELLDSGLSVSQLVKTAWAAASTYRDSDKRGGANGARIRLEPQ
RSWEVNEPDQLDDVLGTLEAIQASFNDAQSDDTRVSLADLIVLGGAAAVEQAAADAGYDV
EVPFEPGRTDASQEQTDVESFEMLKPDADGFRNYIADDVEERPEDLLVDKADLLALSAHE
MTVLVGGMRALGANYQDSDLGVLTDEPETLTNDFFVNLLDMDYKWEPVSDDEYLYEVRDR
ETGDVEWEATRFDLIFGSNSRLRAIAEVYGGDDGEEEFVEDFVETWHKVMSHDRFDLE

Enzyme Prediction     

No EC number prediction in MGYG000001639_00509.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	62	174	4.6e-16	0.43137254901960786

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR00198	cat_per_HPI	0.0	3	717	14	713	catalase/peroxidase HPI. As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]
COG0376	KatG	0.0	4	718	30	730	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
cd00649	catalase_peroxidase_1	0.0	2	412	3	407	N-terminal catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.
PRK15061	PRK15061	0.0	4	718	17	726	catalase/peroxidase.
cd08200	catalase_peroxidase_2	9.14e-176	418	714	1	297	C-terminal non-catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QZY04649.1	0.0	1	718	1	715
QPC71243.1	7.75e-263	7	718	60	774
BCS01357.1	2.09e-32	42	394	6	265
BCS13101.1	2.09e-32	42	394	6	265
QMW47926.1	8.08e-29	42	394	6	265

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3UW8_A	0.0	4	718	22	731	CrystalStructure Analysis of the Ser305Thr Variants of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3UW8_B Crystal Structure Analysis of the Ser305Thr Variants of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049]
1ITK_A	0.0	4	718	22	731	Crystalstructure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui],1ITK_B Crystal structure of catalase-peroxidase from Haloarcula marismortui [Haloarcula marismortui]
3VLM_A	0.0	4	718	22	731	CrystalStructure Analysis of the Met244Ala Variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3VLM_B Crystal Structure Analysis of the Met244Ala Variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049]
3VLH_A	0.0	4	718	22	731	CrystalStructure Analysis of the Arg409Leu Variants of KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLH_B Crystal Structure Analysis of the Arg409Leu Variants of KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLI_A Crystal Structure Analysis of the Cyanide Arg409Leu Variant KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLI_B Crystal Structure Analysis of the Cyanide Arg409Leu Variant KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLJ_A Crystal Structure Analysis of the Cyanide Arg409Leu Variant Complexes with o-Dianisidine in KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049],3VLJ_B Crystal Structure Analysis of the Cyanide Arg409Leu Variant Complexes with o-Dianisidine in KatG from HALOARCULA MARISMORTUI [Haloarcula marismortui ATCC 43049]
3VLK_A	0.0	4	718	22	731	CrystalStructure Analysis of the Ser305Ala variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3VLK_B Crystal Structure Analysis of the Ser305Ala variant of KatG from Haloarcula marismortui [Haloarcula marismortui ATCC 43049],3VLL_A Crystal Structure Analysis of the Ser305Ala variant of KatG from HALOARCULA MARISMORTUI Complexes with Inhibitor SHA [Haloarcula marismortui ATCC 43049],3VLL_B Crystal Structure Analysis of the Ser305Ala variant of KatG from HALOARCULA MARISMORTUI Complexes with Inhibitor SHA [Haloarcula marismortui ATCC 43049]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q3IQZ9	0.0	9	718	9	713	Catalase-peroxidase OS=Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara) OX=348780 GN=katG PE=3 SV=1
O73955	0.0	1	718	1	720	Catalase-peroxidase OS=Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) OX=64091 GN=katG PE=3 SV=1
Q24YU1	0.0	7	717	25	729	Catalase-peroxidase OS=Desulfitobacterium hafniense (strain Y51) OX=138119 GN=katG PE=3 SV=1
Q2RZX7	0.0	1	718	15	729	Catalase-peroxidase OS=Salinibacter ruber (strain DSM 13855 / M31) OX=309807 GN=katG PE=3 SV=1
O59651	0.0	4	718	22	731	Catalase-peroxidase 2 OS=Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) OX=272569 GN=katG2 PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000039	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001639_00509.