ID V2TQJ3_9GAMM Unreviewed; 505 AA.
AC V2TQJ3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Catalase A {ECO:0000313|EMBL:ESK38280.1};
GN ORFNames=P256_01811 {ECO:0000313|EMBL:ESK38280.1};
OS Acinetobacter nectaris CIP 110549.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1392540 {ECO:0000313|EMBL:ESK38280.1, ECO:0000313|Proteomes:UP000023785};
RN [1] {ECO:0000313|EMBL:ESK38280.1, ECO:0000313|Proteomes:UP000023785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110549 {ECO:0000313|EMBL:ESK38280.1,
RC ECO:0000313|Proteomes:UP000023785};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter nectaris CIP 110549.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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=1.11.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000720};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK38280.1}.
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DR EMBL; AYER01000007; ESK38280.1; -; Genomic_DNA.
DR RefSeq; WP_023273437.1; NZ_KI530734.1.
DR AlphaFoldDB; V2TQJ3; -.
DR STRING; 1392540.P256_01811; -.
DR PATRIC; fig|1392540.3.peg.1749; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_6; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000023785; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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; cd08156; catalase_clade_3; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF61; CATALASE; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038928-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000023785}.
FT DOMAIN 9..394
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 339
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-2"
SQ SEQUENCE 505 AA; 58006 MW; C16A2A96D80BFA47 CRC64;
MSKCPYHQTT TAGSPIADNQ NSLSVDSRGP LLLQDWQLIE KLAHQNRERI PERTVHAKGW
GAFGTFKLTK DLSEYTRAKI FNGVGKETKM LARFSTVAGE MGAADAERDV RGFSLKFYTE
EGNWDLVGNN TPVFFIRDPL KFPDFIHTQK RHPRTNLRSP TAMWDFWSQS PESLHQVTIL
MSDRGLPTDV RHMNGYGSHT YSFWNENGER FWVKFHFKTQ QGHRHWTNPE GQQKVGESRE
TTQEDLYYSI ENGDYPKWTV QVQIMPELDA EKTSYNPFDL TKVWPHADYP PIEIGVLELN
HNPENYFAQI EQAAFSPSNA VPGIGFSPDK VLQARVFSYA DAHRYRLGTH YENIPVNRPI
CPVHHYHKDG QMNIQEHFPN PDAYYEPNSF GGPTQNPDVK EPPLKLNSNI VDRFNHREDE
GNNDYIQVTG LFNLFDDGEK SRLFSNIADA MQGVPKEIIE RQLVHFSRIN PDYETGVRKA
LHASGHSSYQ QQDGHITEQT DGHSE
//
