ID A0A0Q9CWY2_9CELL Unreviewed; 220 AA.
AC A0A0Q9CWY2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Heme oxygenase {ECO:0000313|EMBL:KRD47643.1};
GN ORFNames=ASE27_00830 {ECO:0000313|EMBL:KRD47643.1};
OS Oerskovia sp. Root918.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Oerskovia.
OX NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD47643.1, ECO:0000313|Proteomes:UP000051694};
RN [1] {ECO:0000313|EMBL:KRD47643.1, ECO:0000313|Proteomes:UP000051694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root918 {ECO:0000313|EMBL:KRD47643.1,
RC ECO:0000313|Proteomes:UP000051694};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD47643.1, ECO:0000313|Proteomes:UP000051694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root918 {ECO:0000313|EMBL:KRD47643.1,
RC ECO:0000313|Proteomes:UP000051694};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRD47643.1}.
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DR EMBL; LMJG01000001; KRD47643.1; -; Genomic_DNA.
DR RefSeq; WP_056646483.1; NZ_LMJG01000001.1.
DR AlphaFoldDB; A0A0Q9CWY2; -.
DR Proteomes; UP000051694; Unassembled WGS sequence.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006788; P:heme oxidation; IEA:InterPro.
DR CDD; cd19165; HemeO; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR InterPro; IPR002051; Haem_Oase.
DR InterPro; IPR016053; Haem_Oase-like.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR PANTHER; PTHR10720; HEME OXYGENASE; 1.
DR PANTHER; PTHR10720:SF0; HEME OXYGENASE; 1.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR PIRSF; PIRSF000343; Haem_Oase; 1.
DR PRINTS; PR00088; HAEMOXYGNASE.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR000343-1};
KW Iron {ECO:0000256|PIRSR:PIRSR000343-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000343-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051694}.
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 27
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 /evidence="ECO:0000256|PIRSR:PIRSR000343-2"
FT BINDING 134
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 181
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ SEQUENCE 220 AA; 24177 MW; 59CBC4B99907C84C CRC64;
MTAETLPPAP APASLSLRLR EGTRPEHEQA ETTGFVEKLM GGELDVAAYT DLAAQQYAIY
GALERASAQI RDDAQGATLV FDELTRTPSI EKDLAFLVGS DWATEIRILP ATEAYVARLL
EVGTSLSAYA AHAYTRYLGD LSGGQIIKRM MERHYGLGPD GLAFYTFDEI PKAKPFKDVY
RERLDSLDLT DEQIAETVEE AKLAFRLNSA LFAELGAIHC
//
