ID   HBL_HORVU               Reviewed;         162 AA.
AC   Q42831; O04992;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Non-symbiotic hemoglobin;
DE   AltName: Full=HORvu GLB1;
DE   AltName: Full=Non-legume hemoglobin;
GN   Name=HB; Synonyms=GLB1;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Harrington; TISSUE=Aleurone;
RX   PubMed=8204823; DOI=10.1007/bf00014440;
RA   Taylor E.R., Nie X.Z., Macgregor A.W., Hill R.D.;
RT   "A cereal haemoglobin gene is expressed in seed and root tissues under
RT   anaerobic conditions.";
RL   Plant Mol. Biol. 24:853-862(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Harrington;
RA   Guy P.A., Sowa A.W., Hill R.D.;
RT   "Genomic nucleotide sequence of the barley hemoglobin gene.";
RL   (er) Plant Gene Register PGR97-093(1997).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=9201978; DOI=10.1074/jbc.272.27.16746;
RA   Duff S.M.G., Wittenberg J.B., Hill R.D.;
RT   "Expression, purification, and properties of recombinant barley (Hordeum
RT   sp.) hemoglobin. Optical spectra and reactions with gaseous ligands.";
RL   J. Biol. Chem. 272:16746-16752(1997).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CYANIDE, AND
RP   IRON-BINDING SITES.
RX   PubMed=17560601; DOI=10.1016/j.jmb.2007.05.029;
RA   Hoy J.A., Robinson H., Trent J.T. III, Kakar S., Smagghe B.J.,
RA   Hargrove M.S.;
RT   "Plant hemoglobins: a molecular fossil record for the evolution of oxygen
RT   transport.";
RL   J. Mol. Biol. 371:168-179(2007).
CC   -!- FUNCTION: May not function as an oxygen storage or transport protein,
CC       but might act as an oxygen sensor or play a role in electron transfer,
CC       possibly to a bound oxygen molecule.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:17560601}.
CC   -!- TISSUE SPECIFICITY: Seeds and roots.
CC   -!- INDUCTION: Under anaerobic conditions.
CC   -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U01228; AAA19576.1; -; mRNA.
DR   EMBL; U94968; AAB70097.1; -; Genomic_DNA.
DR   PIR; S46502; S46502.
DR   PDB; 2OIF; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-162.
DR   PDBsum; 2OIF; -.
DR   AlphaFoldDB; Q42831; -.
DR   SMR; Q42831; -.
DR   EnsemblPlants; HORVU.MOREX.r2.4HG0328580.1; HORVU.MOREX.r2.4HG0328580.1; HORVU.MOREX.r2.4HG0328580.
DR   EnsemblPlants; HORVU.MOREX.r2.4HG0328580.1.mrna1; HORVU.MOREX.r2.4HG0328580.1.mrna1; HORVU.MOREX.r2.4HG0328580.1.
DR   Gramene; HORVU.MOREX.r2.4HG0328580.1; HORVU.MOREX.r2.4HG0328580.1; HORVU.MOREX.r2.4HG0328580.
DR   Gramene; HORVU.MOREX.r2.4HG0328580.1.mrna1; HORVU.MOREX.r2.4HG0328580.1.mrna1; HORVU.MOREX.r2.4HG0328580.1.
DR   OMA; NAPPRYY; -.
DR   EvolutionaryTrace; Q42831; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR001032; Leghaemoglobin.
DR   InterPro; IPR019824; Leghaemoglobin_Fe_BS.
DR   PANTHER; PTHR22924; PTHR22924; 1.
DR   Pfam; PF00042; Globin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
DR   PROSITE; PS00208; PLANT_GLOBIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Heme; Iron; Metal-binding.
FT   CHAIN           1..162
FT                   /note="Non-symbiotic hemoglobin"
FT                   /id="PRO_0000193016"
FT   BINDING         70
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="distal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         105
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   HELIX           15..25
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           29..43
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           45..50
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           65..83
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           85..88
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           98..107
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           112..129
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:2OIF"
FT   HELIX           137..156
FT                   /evidence="ECO:0007829|PDB:2OIF"
SQ   SEQUENCE   162 AA;  18043 MW;  5386D78AD960757E CRC64;
     MSAAEGAVVF SEEKEALVLK SWAIMKKDSA NLGLRFFLKI FEIAPSARQM FPFLRDSDVP
     LETNPKLKTH AVSVFVMTCE AAAQLRKAGK ITVRETTLKR LGGTHLKYGV ADGHFEVTRF
     ALLETIKEAL PADMWGPEMR NAWGEAYDQL VAAIKQEMKP AE