HEMT_THEDY
ID HEMT_THEDY Reviewed; 113 AA.
AC P02246;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Hemerythrin;
OS Themiste dyscrita (Peanut worm) (Dendrostomum dyscritum).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Sipuncula; Sipunculidea;
OC Golfingiida; Themistidae; Themiste.
OX NCBI_TaxID=6436;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=670224; DOI=10.1016/s0021-9258(17)30328-9;
RA Loehr J.S., Lammers P.J., Brimhall B., Hermodson M.A.;
RT "Amino acid sequence of hemerythrin from Themiste dyscritum.";
RL J. Biol. Chem. 253:5726-5731(1978).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND IRON LIGANDS.
RX PubMed=678527; DOI=10.1021/bi00606a007;
RA Stenkamp R.E., Sieker L.C., Jensen L.H., McQueen J.E. Jr.;
RT "Structure of methemerythrin at 2.8-A resolution: computer graphics fit of
RT an averaged electron density map.";
RL Biochemistry 17:2499-2504(1978).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND IRON LIGANDS.
RA Stenkamp R.E., Sieker L.C., Jensen L.H., Sanders-Loehr J.;
RT "Structure of the binuclear iron complex in metazidohaemerythrin from
RT Themiste dyscritum at 2.2-A resolution.";
RL Nature 291:263-264(1981).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) IN COMPLEX WITH IRON.
RX PubMed=1870128; DOI=10.1016/0022-2836(91)90113-k;
RA Holmes M.A., Stenkamp R.E.;
RT "Structures of met and azidomet hemerythrin at 1.66-A resolution.";
RL J. Mol. Biol. 220:723-737(1991).
CC -!- FUNCTION: Hemerythrin is a respiratory protein in blood cells of
CC certain marine worms. The oxygen-binding site in each chain contains
CC two iron atoms.
CC -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:P02244}.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR PIR; A92234; HRTHBD.
DR PDB; 1HMD; X-ray; 2.00 A; A/B/C/D=1-113.
DR PDB; 1HMO; X-ray; 2.00 A; A/B/C/D=1-113.
DR PDB; 2HMQ; X-ray; 1.66 A; A/B/C/D=1-113.
DR PDB; 2HMZ; X-ray; 1.66 A; A/B/C/D=1-113.
DR PDBsum; 1HMD; -.
DR PDBsum; 1HMO; -.
DR PDBsum; 2HMQ; -.
DR PDBsum; 2HMZ; -.
DR AlphaFoldDB; P02246; -.
DR SMR; P02246; -.
DR EvolutionaryTrace; P02246; -.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.50; -; 1.
DR InterPro; IPR002063; Haemerythrin.
DR InterPro; IPR016131; Haemerythrin_Fe_BS.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
DR PIRSF; PIRSF002033; Hemerythrin; 1.
DR PRINTS; PR00186; HEMERYTHRIN.
DR SUPFAM; SSF47188; SSF47188; 1.
DR TIGRFAMs; TIGR02481; hemeryth_dom; 1.
DR TIGRFAMs; TIGR00058; Hemerythrin; 1.
DR PROSITE; PS00550; HEMERYTHRINS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Iron; Metal-binding;
KW Oxygen transport; Transport.
FT CHAIN 1..113
FT /note="Hemerythrin"
FT /id="PRO_0000191839"
FT BINDING 25
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:1870128,
FT ECO:0000269|PubMed:678527, ECO:0007744|PDB:1HMD,
FT ECO:0007744|PDB:1HMO, ECO:0007744|PDB:2HMQ"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:1870128,
FT ECO:0000269|PubMed:678527, ECO:0007744|PDB:1HMD,
FT ECO:0007744|PDB:1HMO, ECO:0007744|PDB:2HMQ"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:1870128,
FT ECO:0007744|PDB:1HMD, ECO:0007744|PDB:1HMO,
FT ECO:0007744|PDB:2HMQ"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:1870128,
FT ECO:0007744|PDB:1HMD, ECO:0007744|PDB:1HMO,
FT ECO:0007744|PDB:2HMQ"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:1870128,
FT ECO:0000269|PubMed:678527, ECO:0007744|PDB:1HMD,
FT ECO:0007744|PDB:1HMO, ECO:0007744|PDB:2HMQ"
FT BINDING 77
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:1870128,
FT ECO:0000269|PubMed:678527, ECO:0007744|PDB:1HMD,
FT ECO:0007744|PDB:1HMO, ECO:0007744|PDB:2HMQ"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:1870128,
FT ECO:0000269|PubMed:678527, ECO:0007744|PDB:1HMD,
FT ECO:0007744|PDB:1HMO, ECO:0007744|PDB:2HMQ"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:1870128,
FT ECO:0007744|PDB:1HMD, ECO:0007744|PDB:1HMO,
FT ECO:0007744|PDB:2HMQ"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:1870128,
FT ECO:0007744|PDB:1HMD, ECO:0007744|PDB:1HMO,
FT ECO:0007744|PDB:2HMQ"
FT VARIANT 64
FT /note="A -> S"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1HMD"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:1HMD"
FT HELIX 41..64
FT /evidence="ECO:0007829|PDB:1HMD"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:1HMD"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:1HMD"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1HMD"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1HMD"
SQ SEQUENCE 113 AA; 13319 MW; 42A133F08738D03A CRC64;
GFPIPDPYCW DISFRTFYTI VDDEHKTLFN GILLLSQADN ADHLNELRRC TGKHFLNEQQ
LMQASQYAGY AEHKKAHDDF IHKLDTWDGD VTYAKNWLVN HIKTIDFKYR GKI
