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HBL1_ORYSJ
ID   HBL1_ORYSJ              Reviewed;         166 AA.
AC   O04986; Q10PH5; Q7G715;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Non-symbiotic hemoglobin 1;
DE   AltName: Full=ORYsa GLB1a;
DE   AltName: Full=rHb1;
GN   Name=HB1; Synonyms=GLB1A; OrderedLocusNames=Os03g0233900, LOC_Os03g13140;
GN   ORFNames=OJ1175C11.5, OsJ_10047 {ECO:0000312|EMBL:EAZ26180.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION, AND MUTAGENESIS
RP   OF HIS-74.
RC   STRAIN=cv. Jackson;
RX   PubMed=9390447; DOI=10.1104/pp.115.3.1259;
RA   Arredondo-Peter R., Hargrove M.S., Sarath G., Moran J.F., Lohrman J.,
RA   Olson J.S., Klucas R.V.;
RT   "Rice hemoglobins. Gene cloning, analysis, and O2-binding kinetics of a
RT   recombinant protein synthesized in Escherichia coli.";
RL   Plant Physiol. 115:1259-1266(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RA   Lira-Ruan V., Ross E.J.H., Sarath G., Klucas R.V., Arredondo-Peter R.;
RT   "Mapping and analysis of a hemoglobin gene family from rice (Oryza
RT   sativa).";
RL   Plant Physiol. Biochem. 40:199-202(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [9]
RP   CHARACTERIZATION, AND MUTAGENESIS OF VAL-47; SER-50; GLU-120 AND VAL-121.
RX   PubMed=11106662; DOI=10.1074/jbc.m009254200;
RA   Goodman M.D., Hargrove M.S.;
RT   "Quaternary structure of rice nonsymbiotic hemoglobin.";
RL   J. Biol. Chem. 276:6834-6839(2001).
RN   [10]
RP   INDUCTION.
RC   STRAIN=cv. Jackson;
RX   PubMed=11448759; DOI=10.1016/s0168-9452(01)00411-3;
RA   Lira-Ruan V., Sarath G., Klucas R.V., Arredondo-Peter R.;
RT   "Synthesis of hemoglobins in rice (Oryza sativa var. Jackson) plants
RT   growing in normal and stress conditions.";
RL   Plant Sci. 161:279-287(2001).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX   PubMed=10986467; DOI=10.1016/s0969-2126(00)00194-5;
RA   Hargrove M.S., Brucker E.A., Stec B., Sarath G., Arredondo-Peter R.,
RA   Klucas R.V., Olson J.S., Phillips G.N. Jr.;
RT   "Crystal structure of a nonsymbiotic plant hemoglobin.";
RL   Structure 8:1005-1014(2000).
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. Has an unusually high affinity for
CC       O(2) because of a very low dissociation constant.
CC   -!- SUBUNIT: Homodimer.
CC   -!- TISSUE SPECIFICITY: Expressed in coleoptiles, embryos, leaves and
CC       roots.
CC   -!- INDUCTION: By flooding and etiolating but not by oxidative, nitrosative
CC       or hormonal stresses. {ECO:0000269|PubMed:11448759}.
CC   -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR   EMBL; U76030; AAC49883.1; -; mRNA.
DR   EMBL; U76029; AAC49882.1; -; Genomic_DNA.
DR   EMBL; AF335504; AAK72229.1; -; Genomic_DNA.
DR   EMBL; AC103891; AAM19125.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF94821.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF11390.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS83133.1; -; Genomic_DNA.
DR   EMBL; CM000140; EAZ26180.1; -; Genomic_DNA.
DR   EMBL; AK064054; BAG88986.1; -; mRNA.
DR   PIR; T04163; T04163.
DR   RefSeq; XP_015629794.1; XM_015774308.1.
DR   PDB; 1D8U; X-ray; 2.35 A; A/B=1-166.
DR   PDB; 2GNV; X-ray; 2.30 A; A/B=2-166.
DR   PDB; 2GNW; X-ray; 2.40 A; A/B=2-166.
DR   PDBsum; 1D8U; -.
DR   PDBsum; 2GNV; -.
DR   PDBsum; 2GNW; -.
DR   AlphaFoldDB; O04986; -.
DR   SMR; O04986; -.
DR   STRING; 4530.OS03T0233900-01; -.
DR   PaxDb; O04986; -.
DR   PRIDE; O04986; -.
DR   EnsemblPlants; Os03t0233900-01; Os03t0233900-01; Os03g0233900.
DR   GeneID; 4332166; -.
DR   Gramene; Os03t0233900-01; Os03t0233900-01; Os03g0233900.
DR   KEGG; osa:4332166; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   HOGENOM; CLU_003827_11_2_1; -.
DR   InParanoid; O04986; -.
DR   OMA; QRMEEAC; -.
DR   OrthoDB; 1379813at2759; -.
DR   BioCyc; MetaCyc:MON-19374; -.
DR   EvolutionaryTrace; O04986; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000007752; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   Genevisible; O04986; OS.
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; Reference proteome.
FT   CHAIN           1..166
FT                   /note="Non-symbiotic hemoglobin 1"
FT                   /id="PRO_0000193021"
FT   BINDING         74
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   BINDING         109
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   MUTAGEN         47
FT                   /note="V->N: Prevents subunit association, but has little
FT                   effect on ligand binding."
FT                   /evidence="ECO:0000269|PubMed:11106662"
FT   MUTAGEN         50
FT                   /note="S->A: Prevents subunit association, but has little
FT                   effect on ligand binding."
FT                   /evidence="ECO:0000269|PubMed:11106662"
FT   MUTAGEN         74
FT                   /note="H->L: Increases 1000 times the dissociation constant
FT                   of O(2)."
FT                   /evidence="ECO:0000269|PubMed:9390447"
FT   MUTAGEN         120
FT                   /note="E->V: Prevents subunit association, but has little
FT                   effect on ligand binding."
FT                   /evidence="ECO:0000269|PubMed:11106662"
FT   MUTAGEN         121
FT                   /note="V->N: Prevents subunit association, but has little
FT                   effect on ligand binding."
FT                   /evidence="ECO:0000269|PubMed:11106662"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:1D8U"
FT   HELIX           16..29
FT                   /evidence="ECO:0007829|PDB:2GNV"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:2GNV"
FT   HELIX           33..47
FT                   /evidence="ECO:0007829|PDB:2GNV"
FT   HELIX           49..53
FT                   /evidence="ECO:0007829|PDB:2GNV"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:2GNV"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:2GNV"
FT   HELIX           69..92
FT                   /evidence="ECO:0007829|PDB:2GNV"
FT   HELIX           99..111
FT                   /evidence="ECO:0007829|PDB:2GNV"
FT   HELIX           116..133
FT                   /evidence="ECO:0007829|PDB:2GNV"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:2GNV"
FT   HELIX           141..160
FT                   /evidence="ECO:0007829|PDB:2GNV"
SQ   SEQUENCE   166 AA;  18444 MW;  C1FE2CA4701682EF CRC64;
     MALVEDNNAV AVSFSEEQEA LVLKSWAILK KDSANIALRF FLKIFEVAPS ASQMFSFLRN
     SDVPLEKNPK LKTHAMSVFV MTCEAAAQLR KAGKVTVRDT TLKRLGATHL KYGVGDAHFE
     VVKFALLDTI KEEVPADMWS PAMKSAWSEA YDHLVAAIKQ EMKPAE
 
 
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