HBL_ZEAMP
ID HBL_ZEAMP Reviewed; 165 AA.
AC Q9M593;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Non-symbiotic hemoglobin;
DE AltName: Full=Hbt;
DE AltName: Full=ZEAmp GLB1;
GN Name=HB; Synonyms=GLB1;
OS Zea mays subsp. parviglumis (Balsas teosinte).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=76912;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11718894; DOI=10.1016/s0167-4781(01)00288-3;
RA Arechaga-Ocampo E., Saenz-Rivera J., Sarath G., Klucas R.V.,
RA Arredondo-Peter R.;
RT "Cloning and expression analysis of hemoglobin genes from maize (Zea mays
RT ssp. mays) and teosinte (Zea mays ssp. parviglumis).";
RL Biochim. Biophys. Acta 1522:1-8(2001).
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 -!- TISSUE SPECIFICITY: In vegetative but not in embryonic organs.
CC -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR EMBL; AF291052; AAG01183.1; -; Genomic_DNA.
DR PDB; 2R50; X-ray; 2.20 A; A/B/C/D=1-165.
DR PDBsum; 2R50; -.
DR AlphaFoldDB; Q9M593; -.
DR SMR; Q9M593; -.
DR EvolutionaryTrace; Q9M593; -.
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..165
FT /note="Non-symbiotic hemoglobin"
FT /id="PRO_0000193019"
FT BINDING 73
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 108
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..29
FT /evidence="ECO:0007829|PDB:2R50"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:2R50"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:2R50"
FT HELIX 68..91
FT /evidence="ECO:0007829|PDB:2R50"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:2R50"
FT HELIX 115..132
FT /evidence="ECO:0007829|PDB:2R50"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:2R50"
FT HELIX 140..159
FT /evidence="ECO:0007829|PDB:2R50"
SQ SEQUENCE 165 AA; 18278 MW; 35D9EB98D23039ED CRC64;
MALAEADDGA VVFGEEQEAL VLKSWAVMKK DAANLGLRFF LKVFEIAPSA KQMFSFLRDS
DVPLEKNPKL KTHAMSVFVM TCEAAAQLRK AGKVTVRETT LKRLGATHLR YGVADGHFEV
TGFALLETIK EALPADMWSL EMKKAWAEAY SQLVAAIKRE MKPDA