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   03-AUG-2022, entry version 98.
DE   RecName: Full=Leghemoglobin 2;
DE   AltName: Full=Srglb2;
GN   Name=GLB2;
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].
RC   TISSUE=Leaf;
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: Provides oxygen to the bacteroids. This role is essential for
CC       symbiotic nitrogen fixation.
CC   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Root nodules.
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: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   Direct protein sequencing; Heme; Iron; Metal-binding; Nitrogen fixation;
KW   Oxygen transport; 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   BINDING         63
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         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   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