(data stored in ACNUC7421 zone)

HOGENOM: STAAN_1_PE1013

ID   STAAN_1_PE1013                       STANDARD;      PRT;   107 AA.
AC   STAAN_1_PE1013; Q7A649;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Heme-degrading monooxygenase isdG; EC=1.14.99 3;AltName:
DE   Full=Heme oxygenase;AltName: Full=Iron-regulated surface determinant
DE   isdG;AltName: Full=Iron-responsive surface determinant isdG;
DE   (STAAN_1.PE1013).
GN   Name=isdG; OrderedLocusNames=SA0983;
OS   STAPHYLOCOCCUS AUREUS SUBSP. AUREUS N315.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAAN_1.PE1013.
CC       Staphylococcus aureus subsp. aureus N315, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:ISDG_STAAN
CC   -!- FUNCTION: Allows bacterial pathogens to use the host heme as an
CC       iron source. Catalyzes the oxidative degradation of the heme
CC       macrocyclic porphyrin ring in the presence of a suitable electron
CC       donor such as ascorbate or NADPH--cytochrome P450 reductase, with
CC       subsequent release of free iron (By similarity).
CC   -!- CATALYTIC ACTIVITY: Heme + 3 AH(2) + 3 O(2) = biliverdin + Fe(2+)
CC       + CO + 3 A + 3 H(2)O.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the antibiotic biosynthesis monooxygenase
CC       family. Heme-degrading monooxygenase isdG subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB42232.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000008026 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q7A649; -.
DR   EMBL; BA000018; BAB42232.1; ALT_INIT; Genomic_DNA.
DR   PIR; D89884; D89884.
DR   RefSeq; NP_374253.2; NC_002745.2.
DR   PDB; 2ZDO; X-ray; 1.80 A; A/B/C/D=1-107.
DR   PDBsum; 2ZDO; -.
DR   ProteinModelPortal; Q7A649; -.
DR   STRING; Q7A649; -.
DR   EnsemblBacteria; EBSTAT00000000416; EBSTAP00000000416; EBSTAG00000000416.
DR   GeneID; 1123810; -.
DR   GenomeReviews; BA000018_GR; SA0983.
DR   KEGG; sau:SA0983; -.
DR   eggNOG; COG2329; -.
DR   GeneTree; EBGT00050000024362; -.
DR   ProtClustDB; PRK13312; -.
DR   BioCyc; SAUR158879:SA0983-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   GO; GO:0033212; P:iron assimilation; IEA:InterPro.
DR   HAMAP; MF_01272; IsdG; 1; -.
DR   InterPro; IPR007138; Antibiotic_mOase.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR023953; Heme-degrad_mOase.
DR   Pfam; PF03992; ABM; 1.
DR   SUPFAM; SSF54909; Dimer_A_B_barrel; 1.
DR   HOGENOMDNA; STAAN_1.PE1013; -.
KW   3D-structure; Complete proteome; Cytoplasm; Heme; Iron; Metal-binding;
KW   Monooxygenase; Oxidoreductase.
SQ   SEQUENCE   107 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKFMAENRLT LTKGTAKDII ERFYTRHGIE TLEGFDGMFV TQTLEQEDFD EVKILTVWKS
     KQAFTDWLKS DVFKAAHKHV RSKNEDESSP IINNKVITYD IGYSYMK
//

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