ID   GLB_PAREP               Reviewed;         148 AA.
AC   P80721;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Globin-3;
DE   AltName: Full=Myoglobin;
OS   Paramphistomum epiclitum.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Pronocephalata; Paramphistomoidea;
OC   Paramphistomidae; Paramphistomum.
OX   NCBI_TaxID=54403;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-148, AND MASS SPECTROMETRY.
RX   PubMed=9006947; DOI=10.1074/jbc.272.5.2992;
RA   Rashid A.R., van Hauwaert M.-L., Haque M., Siddiqi A.H., Lasters I.,
RA   de Maeyer M., Griffon N., Marden M.C., Dewilde S., Clauwaert J.,
RA   Vinogradov S.N., Moens L.;
RT   "Trematode myoglobins, functional molecules with a distal tyrosine.";
RL   J. Biol. Chem. 272:2992-2999(1997).
RN   [2]
RP   STRUCTURE BY NMR OF THE HEME POCKET RESIDUES.
RX   PubMed=9006948; DOI=10.1074/jbc.272.5.3000;
RA   Zhang W., Rashid K.A., Haque M., Siddiqi A.H., Vinogradov S.N., Moens L.,
RA   la Mar G.N.;
RT   "Solution of 1H NMR structure of the heme cavity in the oxygen-avid
RT   myoglobin from the trematode Paramphistomum epiclitum.";
RL   J. Biol. Chem. 272:3000-3006(1997).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.17 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=11399085; DOI=10.1006/jmbi.2001.4731;
RA   Pesce A., Dewilde S., Kiger L., Milani M., Ascenzi P., Marden M.C.,
RA   Van Hauwaert M.L., Vanfleteren J., Moens L., Bolognesi M.;
RT   "Very high resolution structure of a trematode hemoglobin displaying a
RT   TyrB10-TyrE7 heme distal residue pair and high oxygen affinity.";
RL   J. Mol. Biol. 309:1153-1164(2001).
CC   -!- FUNCTION: Oxygen binding protein.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11399085}.
CC   -!- MASS SPECTROMETRY: Mass=16643.2; Mass_error=1.58; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9006947};
CC   -!- MISCELLANEOUS: This globin lacks one of the heme-binding histidine
CC       residues found in most other globins (replaced by a tyrosine) but has
CC       an extreme oxygen-avidity and high oxidation resistance despite this
CC       change.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000305}.
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DR   PIR; A58345; A58345.
DR   PDB; 1H97; X-ray; 1.17 A; A/B=2-148.
DR   PDB; 1KFR; X-ray; 1.85 A; A=2-148.
DR   PDBsum; 1H97; -.
DR   PDBsum; 1KFR; -.
DR   AlphaFoldDB; P80721; -.
DR   SMR; P80721; -.
DR   EvolutionaryTrace; P80721; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd01040; Mb-like; 1.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR011406; Globin_trematode.
DR   InterPro; IPR044399; Mb-like_M.
DR   Pfam; PF00042; Globin; 1.
DR   PIRSF; PIRSF036488; Myoglobin_tremt; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..148
FT                   /note="Globin-3"
FT                   /id="PRO_0000052466"
FT   BINDING         99
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   HELIX           5..15
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   HELIX           16..18
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:1KFR"
FT   HELIX           22..39
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   HELIX           41..46
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   HELIX           62..79
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   TURN            80..83
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   HELIX           85..97
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   TURN            98..101
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   HELIX           106..123
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:1H97"
FT   HELIX           127..145
FT                   /evidence="ECO:0007829|PDB:1H97"
SQ   SEQUENCE   148 AA;  16770 MW;  BA19B66A3E5E5F0D CRC64;
     MTLTKHEQDI LLKELGPHVD TPAHIVETGL GAYHALFTAH PQYIIHFSRL EGHTIENVMQ
     SEGIKHYART LTEAIVHMLK EISNDAEVKK IAAQYGKDHT SRKVTKDEFM SGEPIFTKYF
     QNLVKDAEGK AAVEKFLKHV FPMMAAEI