ID   HBPL_PARAD              Reviewed;         162 AA.
AC   P68168; P04396;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Non-legume hemoglobin;
OS   Parasponia andersonii (Sponia andersonii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX   NCBI_TaxID=3476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Landsmann J., Dennis E.S., Higgins T.J.V., Appleby C.A., Kortt A.A.,
RA   Peacock W.J.;
RT   "Common evolutionary origin of legume and non-legume plant haemoglobins.";
RL   Nature 324:166-168(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 6-160.
RA   Kortt A.A., Burns J.E., Trinick M.J., Appleby C.A.;
RT   "The amino acid sequence of hemoglobin I from Parasponia andersonii, a
RT   nonleguminous plant.";
RL   FEBS Lett. 180:55-60(1985).
RN   [3]
RP   PROTEIN SEQUENCE OF 28-40 AND 67-86, ACETYLATION AT SER-2, SEQUENCE
RP   REVISION, POLYMORPHISM, AND VARIANT ASP-31.
RX   PubMed=3402445; DOI=10.1111/j.1432-1033.1988.tb14176.x;
RA   Kortt A.A., Trinick M.J., Appleby C.A.;
RT   "Amino acid sequences of hemoglobins I and II from root nodules of the non-
RT   leguminous Parasponia rigida-rhizobium symbiosis, and a correction of the
RT   sequence of hemoglobin I from Parasponia andersonii.";
RL   Eur. J. Biochem. 175:141-149(1988).
CC   -!- FUNCTION: Provides oxygen to the bacteroids. This role is essential for
CC       symbiotic nitrogen fixation.
CC   -!- SUBUNIT: Homodimer.
CC   -!- TISSUE SPECIFICITY: Root nodules.
CC   -!- POLYMORPHISM: Two variants of the protein, hemoglobin I and hemoglobin
CC       II seem to exist. {ECO:0000269|PubMed:3402445}.
CC   -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR   EMBL; U27194; AAB86653.1; -; Genomic_DNA.
DR   PIR; S05541; GPDRNL.
DR   PDB; 3QQR; X-ray; 2.16 A; A/B=1-162.
DR   PDBsum; 3QQR; -.
DR   AlphaFoldDB; P68168; -.
DR   SMR; P68168; -.
DR   iPTMnet; P68168; -.
DR   EvolutionaryTrace; P68168; -.
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   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
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; Acetylation; Direct protein sequencing; Heme; Iron;
KW   Metal-binding; Nitrogen fixation; Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..162
FT                   /note="Non-legume hemoglobin"
FT                   /id="PRO_0000192981"
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   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:3402445"
FT   VARIANT         31
FT                   /note="E -> D (in 30% hemoglobin I and in hemoglobin II)"
FT                   /evidence="ECO:0000269|PubMed:3402445"
FT   CONFLICT        91
FT                   /note="A -> V (in Ref. 1; AAB86653)"
FT                   /evidence="ECO:0000305"
FT   HELIX           12..25
FT                   /evidence="ECO:0007829|PDB:3QQR"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:3QQR"
FT   HELIX           29..43
FT                   /evidence="ECO:0007829|PDB:3QQR"
FT   HELIX           45..50
FT                   /evidence="ECO:0007829|PDB:3QQR"
FT   HELIX           52..54
FT                   /evidence="ECO:0007829|PDB:3QQR"
FT   HELIX           67..88
FT                   /evidence="ECO:0007829|PDB:3QQR"
FT   HELIX           95..108
FT                   /evidence="ECO:0007829|PDB:3QQR"
FT   HELIX           112..129
FT                   /evidence="ECO:0007829|PDB:3QQR"
FT   TURN            131..133
FT                   /evidence="ECO:0007829|PDB:3QQR"
FT   HELIX           136..154
FT                   /evidence="ECO:0007829|PDB:3QQR"
SQ   SEQUENCE   162 AA;  18150 MW;  C68B7F8F47E3DFB4 CRC64;
     MSSSEVNKVF TEEQEALVVK AWAVMKKNSA ELGLQFFLKI FEIAPSAKNL FSYLKDSPVP
     LEQNPKLKPH ATTVFVMTCE SAVQLRKAGK ATVKESDLKR IGAIHFKTGV VNEHFEVTRF
     ALLETIKEAV PEMWSPEMKN AWGVAYDQLV AAIKFEMKPS ST