ID   MYG_HALDV               Reviewed;         378 AA.
AC   Q01966; Q26485;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Myoglobin;
OS   Haliotis diversicolor (Abalone) (Sulculus diversicolor).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX   NCBI_TaxID=36095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Aquatilis; TISSUE=Red muscle;
RX   PubMed=1453473; DOI=10.1016/0022-2836(92)90854-d;
RA   Suzuki T., Takagi T.;
RT   "A myoglobin evolved from indoleamine 2,3-dioxygenase.";
RL   J. Mol. Biol. 228:698-700(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8765749; DOI=10.1016/0167-4781(96)00059-0;
RA   Suzuki T., Yuasa H., Imai K.;
RT   "Convergent evolution. The gene structure of Sulculus 41 kDa myoglobin is
RT   homologous with that of human indoleamine dioxygenase.";
RL   Biochim. Biophys. Acta 1308:41-48(1996).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2806465; DOI=10.1007/bf01953061;
RA   Suzuki T., Furukohri T.;
RT   "The ear-shell (Sulculus diversicolor aquatilis) myoglobin is composed of
RT   an unusual 39 kDa polypeptide chain.";
RL   Experientia 45:998-1002(1989).
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;
CC       Note=Binds 1 heme group per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: In the presence of tryptophan, the autoxidation rate of
CC       the protein is greatly accelerated (25 times).
CC   -!- SIMILARITY: Belongs to the indoleamine 2,3-dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; X68336; CAA48412.1; -; mRNA.
DR   EMBL; D83984; BAA18961.1; -; Genomic_DNA.
DR   PIR; S72172; S72172.
DR   AlphaFoldDB; Q01966; -.
DR   SMR; Q01966; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..378
FT                   /note="Myoglobin"
FT                   /id="PRO_0000215207"
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"
FT   MOD_RES         2
FT                   /note="Blocked amino end (Ala)"
FT                   /evidence="ECO:0000269|PubMed:1453473,
FT                   ECO:0000269|PubMed:2806465"
FT   CONFLICT        33
FT                   /note="W -> G (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="L -> G (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="S -> G (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="T -> G (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="G -> A (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="R -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        355
FT                   /note="K -> G (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        374
FT                   /note="E -> Q (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   378 AA;  41106 MW;  D81841E4B11B5B0B CRC64;
     MADIQLSKYH VSKDIGFLLE PLQDVLPDYF APWNRLAKSL PDLVASHKFR DAVKEMPLLD
     SSKLAGYRQK RLAHLQLVLI TSGYLWQEGE GGAVQRLPEC VAKPLWNVSN DLGLKPVLTY
     GDVCLTNCRV KGGDIEVMYN LPGGAGTEWF LKVCGLVELT LGKGAQSVQN VLDGAKANDK
     AKMTSGLTEL TTTIGNMQAA LAKMNDNLTP DHFYNVLRPF LGGFGGPASP ISGGLIYEGV
     SDAPVTMIGG SAAQSSAMQL LDNLLGVTHS PDKQAFLDEI SNYMIPAHKQ LLADLTKMPR
     KVPQIVAEAK DANLSKAYSG CVAALTQYRT YHIQVVTKYI VTASKSDSPK SLAYKDTGKS
     DLIPFLKEVR DDTEKMQK