HMOA_BACSU
ID HMOA_BACSU Reviewed; 108 AA.
AC O31534;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Heme-degrading monooxygenase HmoA;
DE EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
DE AltName: Full=Heme oxygenase;
GN Name=hmoA; Synonyms=yetG; OrderedLocusNames=BSU07150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION, MUTAGENESIS OF ARG-6, 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: Allows bacterial pathogens to use the host heme as an iron
CC source. 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: Repressed by fur in the presence of iron.
CC {ECO:0000269|PubMed:21873409}.
CC -!- DISRUPTION PHENOTYPE: Neither hmoA 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; AL009126; CAB12534.2; -; Genomic_DNA.
DR PIR; D69798; D69798.
DR RefSeq; NP_388596.1; NC_000964.3.
DR RefSeq; WP_003243958.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O31534; -.
DR SMR; O31534; -.
DR STRING; 224308.BSU07150; -.
DR PaxDb; O31534; -.
DR PRIDE; O31534; -.
DR EnsemblBacteria; CAB12534; CAB12534; BSU_07150.
DR GeneID; 936085; -.
DR KEGG; bsu:BSU07150; -.
DR PATRIC; fig|224308.179.peg.775; -.
DR eggNOG; COG2329; Bacteria.
DR OMA; LIRWESE; -.
DR BioCyc; BSUB:BSU07150-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 Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..108
FT /note="Heme-degrading monooxygenase HmoA"
FT /id="PRO_0000360519"
FT DOMAIN 2..95
FT /note="ABM"
FT BINDING 76
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 66
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT MUTAGEN 6
FT /note="R->A: Retains the ability to degrade haem, albeit at
FT a reduced rate relative to the wild-type."
FT /evidence="ECO:0000269|PubMed:21873409"
SQ SEQUENCE 108 AA; 12573 MW; 515C138A29C8812A CRC64;
MFVQLRKMTV KEGFADKVIE RFSAEGIIEK QEGLIDVTVL EKNVRRGDEE VVVMIRWESE
DHWKQWEKSD AHIAGHKANK GKPKPDYLIS TEVSMYHVRA VKQGTYNQ
