ID   LGB2_SESRO              Reviewed;         148 AA.
AC   P14848;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=Leghemoglobin 2 {ECO:0000303|PubMed:3237206, ECO:0000303|Ref.2};
DE            Short=Srglb2 {ECO:0000303|PubMed:3237206, ECO:0000303|Ref.2};
GN   Name=GLB2 {ECO:0000303|PubMed:3237206, ECO:0000303|Ref.2};
OS   Sesbania rostrata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Sesbanieae; Sesbania.
OX   NCBI_TaxID=3895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Leaf, and Stem nodule;
RX   PubMed=3237206; DOI=10.1007/bf00337709;
RA   Metz B.A., Welters P., Hoffmann H.J., Jensen E.O., Schell J.,
RA   de Bruijn F.J.;
RT   "Primary structure and promoter analysis of leghemoglobin genes of the
RT   stem-nodulated tropical legume Sesbania rostrata: conserved coding
RT   sequences, cis-elements and trans-acting factors.";
RL   Mol. Gen. Genet. 214:181-191(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Welters P., Metz B., Schell J., de Bruijn F.J.;
RL   Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-148.
RC   TISSUE=Stem nodule;
RA   Kortt A.A., Strike P.M., Bogusz D., Appleby C.A.;
RT   "The amino acid sequence of leghemoglobin II from Sesbania rostrata stem
RT   nodules.";
RL   Biochem. Int. 15:509-516(1987).
CC   -!- FUNCTION: Leghemoglobin that reversibly binds oxygen O(2) through a
CC       pentacoordinated heme iron (By similarity). In stem nodules,
CC       facilitates the diffusion of oxygen to the bacteroids while preventing
CC       the bacterial nitrogenase from being inactivated by buffering dioxygen,
CC       nitric oxide and carbon monoxide, and promoting the formation of
CC       reactive oxygen species (ROS, e.g. H(2)O(2)) (By similarity). This role
CC       is essential for symbiotic nitrogen fixation (SNF) (By similarity).
CC       {ECO:0000250|UniProtKB:P02237, ECO:0000250|UniProtKB:Q43296}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P02240}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P02240}. Nucleus {ECO:0000250|UniProtKB:P02240}.
CC   -!- TISSUE SPECIFICITY: Stem nodules. {ECO:0000269|PubMed:3237206}.
CC   -!- PTM: Nitrated in effective nodules and particularly in hypoxic
CC       conditions; this mechanism may play a protective role in the symbiosis
CC       by buffering toxic peroxynitrite NO(2)(-). Nitration level decrease
CC       during nodule senescence. {ECO:0000250|UniProtKB:P02234}.
CC   -!- PTM: Phosphorylation at Ser-45 disrupts the molecular environment of
CC       its porphyrin ring oxygen binding pocket, thus leading to a reduced
CC       oxygen consumption and to the delivery of oxygen O(2) to symbiosomes.
CC       {ECO:0000250|UniProtKB:Q3C1F7}.
CC   -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR   EMBL; X13505; CAA31859.1; -; Genomic_DNA.
DR   EMBL; X13815; CAA32044.1; -; Genomic_DNA.
DR   PIR; S08322; GPFJG2.
DR   PIR; S20162; S20162.
DR   AlphaFoldDB; P14848; -.
DR   SMR; P14848; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   CDD; cd08923; class1-2_nsHbs_Lbs; 1.
DR   Gene3D; 1.10.490.10; Globins; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR001032; Leghaemoglobin-like.
DR   InterPro; IPR019824; Leghaemoglobin_Fe_BS.
DR   PANTHER; PTHR22924; LEGHEMOGLOBIN-RELATED; 1.
DR   PANTHER; PTHR22924:SF92; NON-SYMBIOTIC HEMOGLOBIN 2; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00188; PLANTGLOBIN.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
DR   PROSITE; PS00208; PLANT_GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Heme; Iron; Metal-binding; Nitration;
KW   Nitrogen fixation; Nodulation; Nucleus; Oxygen transport; Phosphoprotein;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.3"
FT   CHAIN           2..148
FT                   /note="Leghemoglobin 2"
FT                   /id="PRO_0000193000"
FT   DOMAIN          2..148
FT                   /note="Globin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         45
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   BINDING         63
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   BINDING         66
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   BINDING         95
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   BINDING         98
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P02240"
FT   MOD_RES         30
FT                   /note="Nitrated tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P02234"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3C1F7"
FT   MOD_RES         136
FT                   /note="Nitrated tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P02234"
FT   CONFLICT        5
FT                   /note="E -> D (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="Q -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="N -> H (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37
FT                   /note="A -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="M -> L (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72..74
FT                   /note="RDS -> HDA (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="L -> T (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="N -> I (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="S -> A (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   148 AA;  15800 MW;  949AA649CBE303EE CRC64;
     MGFTEKQEAL VNASYEAFKQ NLPGNSVLFY SFILEKAPAA KGMFSFLKDS DGVPQNNPSL
     QAHAEKVFGL VRDSAAQLRA TGVVVLADAS LGSVHVQKGV LDPHFVVVKE ALLKTLKEAA
     GATWSDEVSN AWEVAYDGLS AAIKKAMS
//