HBPL_PARRI
ID HBPL_PARRI Reviewed; 162 AA.
AC P68169; P04396;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Non-legume hemoglobin;
OS Parasponia rigida.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3477;
RN [1]
RP PROTEIN SEQUENCE OF 2-162, POLYMORPHISM, ACETYLATION AT SER-2, AND VARIANTS
RP ASP-31; GLN-86 AND VAL-151.
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 are called hemoglobin I and
CC hemoglobin II. {ECO:0000269|PubMed:3402445}.
CC -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR PIR; S01019; S01019.
DR PIR; S01020; S01020.
DR AlphaFoldDB; P68169; -.
DR SMR; P68169; -.
DR iPTMnet; P68169; -.
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 Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Nitrogen fixation; Oxygen transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3402445"
FT CHAIN 2..162
FT /note="Non-legume hemoglobin"
FT /id="PRO_0000192982"
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 VARIANT 86
FT /note="R -> Q (in hemoglobin II)"
FT /evidence="ECO:0000269|PubMed:3402445"
FT VARIANT 151
FT /note="A -> V (in some hemoglobin I and in hemoglobin II)"
FT /evidence="ECO:0000269|PubMed:3402445"
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
