ID   MYG_HALMK               Reviewed;         378 AA.
AC   P51537;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Myoglobin;
OS   Haliotis madaka (Giant abalone) (Nordotis madaka).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX   NCBI_TaxID=81897;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Red muscle;
RX   PubMed=8011076; DOI=10.1007/bf01891987;
RA   Suzuki T.;
RT   "Abalone myoglobins evolved from indoleamine dioxygenase: the cDNA-derived
RT   amino acid sequence of myoglobin from Nordotis madaka.";
RL   J. Protein Chem. 13:9-13(1994).
CC   -!- FUNCTION: Serves a reserve supply of oxygen and facilitates the
CC       movement of oxygen within muscles.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 heme group per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the indoleamine 2,3-dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; S73262; AAB31096.1; -; mRNA.
DR   EMBL; D58415; BAA09586.1; -; mRNA.
DR   AlphaFoldDB; P51537; -.
DR   SMR; P51537; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProt.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR   InterPro; IPR000898; Indolamine_dOase.
DR   InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR   PANTHER; PTHR28657; PTHR28657; 1.
DR   Pfam; PF01231; IDO; 1.
DR   SUPFAM; SSF140959; SSF140959; 1.
DR   PROSITE; PS00876; IDO_1; 1.
DR   PROSITE; PS00877; IDO_2; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..378
FT                   /note="Myoglobin"
FT                   /id="PRO_0000215206"
FT   BINDING         332
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  41442 MW;  B89DF8A1D5D11BB7 CRC64;
     MADIQLSKYH VSKDIGFLLE PLQDVLPDYF EPWNRLAKSL PELVASHKFR DAVKEMPLLD
     QSKLAGYRQK RLAHLQLVLI TSGYLWQEGE GGAVQRLPEC VSKPLWNVSN DLGLKPVLTF
     ADICLTNCKV KNGDIEVMYN LPGGAGTEWF LKVCGLVELA FGKSGQAIQN VLDGAKANDK
     AKMASGFTDL TAAIGNMQTA LARMNENLTP EHFYNGVRPF LNGFGGPASP ISGGLVYEGV
     SDKPVTMIGG SAAQSSTMQV LDGLLGITHS PEKQAFLDEI RNYMPPSHKQ MLADLTNMPR
     KVPQVVAETK DANLTKAFNG CVAAFVQYRS YHIQVVTKYI VTASKSDSPK SLAYKDTGKS
     DLIPFLKEVR DDTEKVQQ