ID   HO_XANC8                Reviewed;         165 AA.
AC   A0A0H2XEA6;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Heme oxygenase {ECO:0000303|PubMed:27621284};
DE            EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
GN   Name=bphO; OrderedLocusNames=XC_4242;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
RN   [2]
RP   INDUCTION, AND OPERON.
RC   STRAIN=8004;
RX   PubMed=27621284; DOI=10.15252/embr.201541691;
RA   Bonomi H.R., Toum L., Sycz G., Sieira R., Toscani A.M., Gudesblat G.E.,
RA   Leskow F.C., Goldbaum F.A., Vojnov A.A., Malamud F.;
RT   "Xanthomonas campestris attenuates virulence by sensing light through a
RT   bacteriophytochrome photoreceptor.";
RL   EMBO Rep. 17:1565-1577(2016).
CC   -!- FUNCTION: Catalyzes the opening of the heme ring to form the open-chain
CC       tetrapyrrole biliverdin IX with the release of iron and carbon monoxide
CC       (CO). {ECO:0000250|UniProtKB:O48782, ECO:0000305|PubMed:27621284}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC         biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:60344; EC=1.14.14.18;
CC         Evidence={ECO:0000250|UniProtKB:O48782};
CC   -!- INDUCTION: Expressed in dark and light. Part of the bphO-bphP operon
CC       (PubMed:27621284). {ECO:0000269|PubMed:27621284}.
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {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; CP000050; AAY51280.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H2XEA6; -.
DR   SMR; A0A0H2XEA6; -.
DR   EnsemblBacteria; AAY51280; AAY51280; XC_4242.
DR   KEGG; xcb:XC_4242; -.
DR   HOGENOM; CLU_085041_4_0_6; -.
DR   OMA; HFHTCLA; -.
DR   Proteomes; UP000000420; Chromosome.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006788; P:heme oxidation; IEA:InterPro.
DR   Gene3D; 1.20.910.10; -; 1.
DR   InterPro; IPR016053; Haem_Oase-like.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   Pfam; PF01126; Heme_oxygenase; 1.
DR   SUPFAM; SSF48613; SSF48613; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..165
FT                   /note="Heme oxygenase"
FT                   /id="PRO_0000438299"
SQ   SEQUENCE   165 AA;  18359 MW;  B2685AEE21644012 CRC64;
     MMQALGQGHI DADTYAQVLR RHHRLLAGFE EQLSDWLVTL VGSGWQYRRR VPALREDLRV
     LGQPVDAAVP PPASSEAARW GMLYVIEGSQ LGGRVIARML RKRQPGLAHA LHYFELADED
     PAGWRRFQAV LEQRLQSAAA RADAIAGAQA MFAHFHTCLA AEARP