HMOB_BACSU
ID HMOB_BACSU Reviewed; 166 AA.
AC P38049;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Heme-degrading monooxygenase HmoB;
DE EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
DE AltName: Full=Heme oxygenase;
GN Name=hmoB; Synonyms=yhgC, yixC; OrderedLocusNames=BSU10100;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8335642; DOI=10.1128/jb.175.15.4870-4876.1993;
RA Popham D.L., Setlow P.;
RT "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpF
RT gene, which codes for a putative class A high-molecular-weight penicillin-
RT binding protein.";
RL J. Bacteriol. 175:4870-4876(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION, MUTAGENESIS OF ASN-70, DISRUPTION PHENOTYPE, INDUCTION, AND
RP NOMENCLATURE.
RX PubMed=21873409; DOI=10.1099/mic.0.053579-0;
RA Gaballa A., Helmann J.D.;
RT "Bacillus subtilis Fur represses one of two paralogous haem-degrading
RT monooxygenases.";
RL Microbiology 157:3221-3231(2011).
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:0000269|PubMed:21873409}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O48782}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:21873409}.
CC -!- DISRUPTION PHENOTYPE: Neither hmoB single mutant nor the hmoA hmoB
CC double mutant display robust and reproducible phenotypes relative to
CC the wild-type. {ECO:0000269|PubMed:21873409}.
CC -!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
CC family. {ECO:0000305}.
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DR EMBL; L10630; AAA71941.1; -; Genomic_DNA.
DR EMBL; Y14083; CAA74516.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12850.1; -; Genomic_DNA.
DR PIR; B40614; B40614.
DR RefSeq; NP_388891.1; NC_000964.3.
DR RefSeq; WP_003244748.1; NZ_JNCM01000035.1.
DR PDB; 4OZ5; X-ray; 2.71 A; A=1-166.
DR PDBsum; 4OZ5; -.
DR AlphaFoldDB; P38049; -.
DR SMR; P38049; -.
DR STRING; 224308.BSU10100; -.
DR PaxDb; P38049; -.
DR PRIDE; P38049; -.
DR EnsemblBacteria; CAB12850; CAB12850; BSU_10100.
DR GeneID; 939297; -.
DR KEGG; bsu:BSU10100; -.
DR PATRIC; fig|224308.179.peg.1086; -.
DR eggNOG; COG2329; Bacteria.
DR InParanoid; P38049; -.
DR OMA; KVYITYG; -.
DR PhylomeDB; P38049; -.
DR BioCyc; BSUB:BSU10100-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..166
FT /note="Heme-degrading monooxygenase HmoB"
FT /id="PRO_0000049578"
FT DOMAIN 66..153
FT /note="ABM"
FT BINDING 33
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 138
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:0000255"
FT SITE 128
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT MUTAGEN 70
FT /note="N->A: Retains the ability to degrade haem, albeit at
FT a reduced rate relative to the wild-type."
FT /evidence="ECO:0000269|PubMed:21873409"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:4OZ5"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:4OZ5"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:4OZ5"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:4OZ5"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4OZ5"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:4OZ5"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:4OZ5"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4OZ5"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:4OZ5"
FT STRAND 99..121
FT /evidence="ECO:0007829|PDB:4OZ5"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:4OZ5"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4OZ5"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:4OZ5"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4OZ5"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:4OZ5"
SQ SEQUENCE 166 AA; 18828 MW; 480644DF1FA5AD77 CRC64;
MKVYITYGTA DFLKTIVQKH PSENILLMQG QENAILIHET NGDTVFQAPH AYEVIDQVGE
IKHPGFAVLN NIAVTQEGRP LFENRFKNRA GKVENEPGFE AIRVLRPLDS DTYVILTLWE
TESAFQDWQQ SGSYKEAHKK RDTSAGIDTT SIFSRPSYVT TYFAVE
