ID   MHUD_MYCTO              Reviewed;         105 AA.
AC   P9WKH2; F2GKD2; O06156; Q7D578;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Heme oxygenase (mycobilin-producing) {ECO:0000305};
DE            EC=1.14.99.57 {ECO:0000250|UniProtKB:P9WKH3};
DE   AltName: Full=Mycobacterial heme utilization, degrader;
DE            Short=MHUD;
GN   Name=mhuD; OrderedLocusNames=MT3698;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the oxidative degradation of the heme macrocyclic
CC       porphyrin ring in the presence of a suitable electron donor such as
CC       ascorbate or NADPH--cytochrome P450 reductase, with subsequent release
CC       of free iron. {ECO:0000250|UniProtKB:P9WKH3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 AH2 + 2 H(+) + heme b + 3 O2 = 3 A + Fe(2+) + 3 H2O +
CC         mycobilin a; Xref=Rhea:RHEA:52232, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:29033, ChEBI:CHEBI:60344,
CC         ChEBI:CHEBI:136507; EC=1.14.99.57;
CC         Evidence={ECO:0000250|UniProtKB:P9WKH3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 AH2 + 2 H(+) + heme b + 3 O2 = 3 A + Fe(2+) + 3 H2O +
CC         mycobilin b; Xref=Rhea:RHEA:52236, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:29033, ChEBI:CHEBI:60344,
CC         ChEBI:CHEBI:136508; EC=1.14.99.57;
CC         Evidence={ECO:0000250|UniProtKB:P9WKH3};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WKH3}.
CC   -!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
CC       family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48056.1; -; Genomic_DNA.
DR   PIR; E70552; E70552.
DR   RefSeq; WP_003419501.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKH2; -.
DR   SMR; P9WKH2; -.
DR   EnsemblBacteria; AAK48056; AAK48056; MT3698.
DR   GeneID; 45427579; -.
DR   KEGG; mtc:MT3698; -.
DR   PATRIC; fig|83331.31.peg.3981; -.
DR   HOGENOM; CLU_141544_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007138; ABM_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   Pfam; PF03992; ABM; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   PROSITE; PS51725; ABM; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..105
FT                   /note="Heme oxygenase (mycobilin-producing)"
FT                   /id="PRO_0000427654"
FT   DOMAIN          3..92
FT                   /note="ABM"
FT   BINDING         22..26
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
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:0000250|UniProtKB:P9WKH3"
FT   BINDING         83..86
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   SITE            66
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   105 AA;  11185 MW;  19CF8FA845269878 CRC64;
     MPVVKINAIE VPAGAGPELE KRFAHRAHAV ENSPGFLGFQ LLRPVKGEER YFVVTHWESD
     EAFQAWANGP AIAAHAGHRA NPVATGASLL EFEVVLDVGG TGKTA