ID D4YP07_9MICO Unreviewed; 218 AA.
AC D4YP07;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Heme oxygenase {ECO:0000313|EMBL:EFG47147.1};
DE EC=1.14.99.3 {ECO:0000313|EMBL:EFG47147.1};
GN Name=hmuO {ECO:0000313|EMBL:EFG47147.1};
GN ORFNames=HMPREF0183_1667 {ECO:0000313|EMBL:EFG47147.1};
OS Brevibacterium mcbrellneri ATCC 49030.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=585530 {ECO:0000313|EMBL:EFG47147.1, ECO:0000313|Proteomes:UP000005714};
RN [1] {ECO:0000313|EMBL:EFG47147.1, ECO:0000313|Proteomes:UP000005714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49030 {ECO:0000313|EMBL:EFG47147.1,
RC ECO:0000313|Proteomes:UP000005714};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2010) 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:EFG47147.1}.
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DR EMBL; ADNU01000046; EFG47147.1; -; Genomic_DNA.
DR RefSeq; WP_005884873.1; NZ_ADNU01000046.1.
DR AlphaFoldDB; D4YP07; -.
DR STRING; 585530.HMPREF0183_1667; -.
DR eggNOG; COG5398; Bacteria.
DR OrthoDB; 5493802at2; -.
DR Proteomes; UP000005714; 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 Oxidoreductase {ECO:0000313|EMBL:EFG47147.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005714}.
FT BINDING 18
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 25
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 130
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 177
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ SEQUENCE 218 AA; 24709 MW; 8E19038B927F6BC4 CRC64;
MTITTPAAET LSFSQRLRKE TQREHSEAES EKFIVDLMAG RLDRHAYIAL LEQYAVLYPA
LETAVQAAPS DSTVAFFDHP GLARTQAINN DLDYLLGEDR QPPVALEATR FLAEHFQSEV
SPEQLLAHHY LRYLGDLSGG LAIGKLVKRH YSIEDEALNM WRFPGINKPK LFKDDYRAKL
DAVTLTREQQ EAVIAEAELG FRLNKAIFRQ LGETLHVE
//