HMO_LISMO
ID HMO_LISMO Reviewed; 167 AA.
AC Q8Y563;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Heme-degrading monooxygenase {ECO:0000303|PubMed:24598731};
DE EC=1.14.-.- {ECO:0000269|PubMed:24598731};
DE AltName: Full=Heme oxygenase {ECO:0000305};
DE AltName: Full=IsdG-type heme-degradation enzyme {ECO:0000303|PubMed:24598731};
DE Short=Isd-LmHde {ECO:0000303|PubMed:24598731};
GN OrderedLocusNames=lmo2213 {ECO:0000312|EMBL:CAD00291.1};
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963 {ECO:0000312|EMBL:CAD00291.1};
RN [1] {ECO:0000312|EMBL:CAD00291.1, ECO:0000312|Proteomes:UP000000817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000312|Proteomes:UP000000817};
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2] {ECO:0007744|PDB:4KIA}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP HEME-BINDING, SUBUNIT, REGION, MUTAGENESIS OF 1-MET--GLY-50; TYR-53;
RP GLU-71; ILE-73; TYR-87; PHE-126; TRP-129; SER-135; THR-139 AND MET-142, AND
RP CIRCULAR DICHROISM ANALYSIS.
RX PubMed=24598731; DOI=10.1107/s1399004713030794;
RA Duong T., Park K.S., Kim T., Kang S.W., Hahn M.J., Hwang H.-Y., Kim K.K.;
RT "Structural and functional characterization of an Isd-type haem-degradation
RT enzyme from Listeria monocytogenes.";
RL Acta Crystallogr. D 70:615-626(2014).
CC -!- FUNCTION: Catalyzes the degradation of heme to biliverdin in the
CC presence of a suitable electron donor such as ascorbate, with the
CC subsequent release of iron. Hardly any CO is released by the heme
CC degradation reaction. Binds heme (PubMed:24598731). Allows bacterial
CC pathogens to use the host heme as an iron source. Release of iron from
CC heme may play a crucial role in the pathogenicity of L.monocytogenes
CC (Probable). {ECO:0000269|PubMed:24598731, ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24598731}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q2FZE2}.
CC -!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
CC family. {ECO:0000305}.
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DR EMBL; AL591982; CAD00291.1; -; Genomic_DNA.
DR PIR; AE1351; AE1351.
DR RefSeq; NP_465737.1; NC_003210.1.
DR RefSeq; WP_009930965.1; NZ_CP023861.1.
DR PDB; 4KIA; X-ray; 1.75 A; A=1-167.
DR PDBsum; 4KIA; -.
DR AlphaFoldDB; Q8Y563; -.
DR SMR; Q8Y563; -.
DR STRING; 169963.lmo2213; -.
DR PaxDb; Q8Y563; -.
DR EnsemblBacteria; CAD00291; CAD00291; CAD00291.
DR GeneID; 984794; -.
DR KEGG; lmo:lmo2213; -.
DR PATRIC; fig|169963.11.peg.2265; -.
DR eggNOG; COG2329; Bacteria.
DR HOGENOM; CLU_116220_1_0_9; -.
DR OMA; FFHEWKK; -.
DR PhylomeDB; Q8Y563; -.
DR BioCyc; LMON169963:LMO2213-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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..167
FT /note="Heme-degrading monooxygenase"
FT /id="PRO_0000452171"
FT DOMAIN 67..154
FT /note="ABM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01062,
FT ECO:0000305|PubMed:24598731"
FT REGION 1..50
FT /note="Important for catalysis"
FT /evidence="ECO:0000269|PubMed:24598731"
FT SITE 129
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT MUTAGEN 1..50
FT /note="Missing: No effect in heme-binding activity. 67.9%
FT reduction of heme-degrading activity compared to wild-type.
FT Homodimerizes."
FT /evidence="ECO:0000269|PubMed:24598731"
FT MUTAGEN 53
FT /note="Y->A: No effect in heme-degrading activity."
FT /evidence="ECO:0000269|PubMed:24598731"
FT MUTAGEN 71
FT /note="E->A: 36.2% reduction of heme-degrading activity
FT compared to wild-type."
FT /evidence="ECO:0000269|PubMed:24598731"
FT MUTAGEN 73
FT /note="I->R: No effect in heme-binding activity. 28.9%
FT reduction of heme-degrading activity compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:24598731"
FT MUTAGEN 87
FT /note="Y->A: No effect in heme-binding activity. 37.0%
FT reduction of heme-degrading activity compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:24598731"
FT MUTAGEN 126
FT /note="F->R: No effect in heme-binding activity. 24.8%
FT reduction of heme-degrading activity compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:24598731"
FT MUTAGEN 129
FT /note="W->A: 61.9% reduction of heme-degrading activity
FT compared to wild-type."
FT /evidence="ECO:0000269|PubMed:24598731"
FT MUTAGEN 129
FT /note="W->R: No effect in heme-binding activity. 64.6%
FT reduction of heme-degrading activity compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:24598731"
FT MUTAGEN 135
FT /note="S->A: 21.9% reduction of heme-degrading activity
FT compared to wild-type."
FT /evidence="ECO:0000269|PubMed:24598731"
FT MUTAGEN 139
FT /note="T->A: 25.5% reduction of heme-degrading activity
FT compared to wild-type."
FT /evidence="ECO:0000269|PubMed:24598731"
FT MUTAGEN 142
FT /note="M->A: 24.8% reduction of heme-degrading activity
FT compared to wild-type."
FT /evidence="ECO:0000269|PubMed:24598731"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4KIA"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:4KIA"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4KIA"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:4KIA"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:4KIA"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:4KIA"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:4KIA"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:4KIA"
FT STRAND 100..121
FT /evidence="ECO:0007829|PDB:4KIA"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:4KIA"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:4KIA"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4KIA"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4KIA"
SQ SEQUENCE 167 AA; 19466 MW; 676DE70AA9EC68A5 CRC64;
MKKVFITTGT EHYLRQLMAN YTGGNVTLLQ NFSQSLLYQE STGEKLFQEG AEYRVLQSSG
SIKGFGVVVF EYIHLRDEEI PIFLQMYQRA SLHFSETPGL QSTKLTKAMN MNKFLIISFW
DSEVFFHDWK KSPLSKEITN IMRKNNTQSG FSHEDIYHYP EFSHDAK
