HDOX1_STAAN
ID HDOX1_STAAN Reviewed; 107 AA.
AC Q7A649;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Heme oxygenase (staphylobilin-producing) 1 {ECO:0000255|HAMAP-Rule:MF_01272};
DE EC=1.14.99.48 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Heme-degrading monooxygenase 1 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Iron-regulated surface determinant 1 {ECO:0000255|HAMAP-Rule:MF_01272};
DE AltName: Full=Iron-responsive surface determinant 1 {ECO:0000255|HAMAP-Rule:MF_01272};
GN Name=isdG; OrderedLocusNames=SA0983;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-7 IN COMPLEX WITH HEME,
RP FUNCTION, MUTAGENESIS OF ASN-7, AND SUBUNIT.
RX PubMed=18713745; DOI=10.1074/jbc.m709486200;
RA Lee W.C., Reniere M.L., Skaar E.P., Murphy M.E.;
RT "Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading
RT enzymes in Staphylococcus aureus.";
RL J. Biol. Chem. 283:30957-30963(2008).
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 to the oxo-bilirubin chromophore staphylobilins (a
CC mixture of 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin) in the
CC presence of a suitable electron donor such as ascorbate or NADPH--
CC cytochrome P450 reductase, with subsequent release of free iron.
CC {ECO:0000269|PubMed:18713745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + delta-staphylobilin +
CC Fe(2+) + formaldehyde + 4 H2O; Xref=Rhea:RHEA:37039,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:60344, ChEBI:CHEBI:74361;
CC EC=1.14.99.48; Evidence={ECO:0000255|HAMAP-Rule:MF_01272};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + beta-staphylobilin +
CC Fe(2+) + formaldehyde + 4 H2O; Xref=Rhea:RHEA:37363,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:60344, ChEBI:CHEBI:74362;
CC EC=1.14.99.48; Evidence={ECO:0000255|HAMAP-Rule:MF_01272};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01272,
CC ECO:0000269|PubMed:18713745}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01272}.
CC -!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
CC family. Heme-degrading monooxygenase IsdG subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01272}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB42232.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; BA000018; BAB42232.1; ALT_INIT; Genomic_DNA.
DR PIR; D89884; D89884.
DR RefSeq; WP_000670950.1; NC_002745.2.
DR PDB; 2ZDO; X-ray; 1.80 A; A/B/C/D=1-107.
DR PDBsum; 2ZDO; -.
DR AlphaFoldDB; Q7A649; -.
DR SMR; Q7A649; -.
DR EnsemblBacteria; BAB42232; BAB42232; BAB42232.
DR KEGG; sau:SA0983; -.
DR HOGENOM; CLU_141544_2_1_9; -.
DR BioCyc; MetaCyc:MON-20094; -.
DR BRENDA; 1.14.99.48; 3352.
DR EvolutionaryTrace; Q7A649; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042167; P:heme catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0033212; P:iron import into cell; IEA:InterPro.
DR HAMAP; MF_01272; Heme_degrading_monooxygenase; 1.
DR InterPro; IPR007138; ABM_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR023953; IsdG.
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.
FT CHAIN 1..107
FT /note="Heme oxygenase (staphylobilin-producing) 1"
FT /id="PRO_0000270091"
FT DOMAIN 3..92
FT /note="ABM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT BINDING 7
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 22..29
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT BINDING 77
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 SITE 67
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01272"
FT MUTAGEN 7
FT /note="N->A: Absence of oxygenase activity."
FT /evidence="ECO:0000269|PubMed:18713745"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:2ZDO"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:2ZDO"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2ZDO"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:2ZDO"
FT STRAND 47..59
FT /evidence="ECO:0007829|PDB:2ZDO"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:2ZDO"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:2ZDO"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2ZDO"
FT STRAND 91..106
FT /evidence="ECO:0007829|PDB:2ZDO"
SQ SEQUENCE 107 AA; 12546 MW; DB13A134D5EC4FF0 CRC64;
MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD EVKILTVWKS
KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD IGYSYMK
