ID   HBL_MAIZE               Reviewed;         165 AA.
AC   Q9FY42;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Non-symbiotic hemoglobin;
DE   AltName: Full=Hbm;
DE   AltName: Full=ZEAma GLB1;
GN   Name=HB; Synonyms=GLB1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Root;
RA   Guy P.A., Hill R.D.;
RT   "Sequence and analysis of a nonsymbiotic hemoglobin gene from maize.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
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 embryonic organs and at low levels in vegetative
CC       organs.
CC   -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR   EMBL; AY005818; AAG01375.1; -; Genomic_DNA.
DR   EMBL; AF236080; AAF44664.1; -; mRNA.
DR   RefSeq; NP_001104966.1; NM_001111496.1.
DR   AlphaFoldDB; Q9FY42; -.
DR   SMR; Q9FY42; -.
DR   STRING; 4577.GRMZM2G067402_P01; -.
DR   PaxDb; Q9FY42; -.
DR   PRIDE; Q9FY42; -.
DR   GeneID; 541815; -.
DR   KEGG; zma:541815; -.
DR   MaizeGDB; 292897; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   OrthoDB; 1379813at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q9FY42; baseline and differential.
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   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Reference proteome.
FT   CHAIN           1..165
FT                   /note="Non-symbiotic hemoglobin"
FT                   /id="PRO_0000193018"
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   CONFLICT        51
FT                   /note="E -> K (in Ref. 1; AAF44664)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   165 AA;  18279 MW;  3BD9EF32723039ED CRC64;
     MALAEADDGA VVFGEEQEAL VLKSWAVMKK DAANLGLRFF LKVFEIAPSA EQMFSFLRDS
     DVPLEKNPKL KTHAMSVFVM TCEAAAQLRK AGKVTVRETT LKRLGATHLR YGVADGHFEV
     TGFALLETIK EALPADMWSL EMKKAWAEAY SQLVAAIKRE MKPDA