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LGB1_PEA
ID   LGB1_PEA                Reviewed;         148 AA.
AC   P02233;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Leghemoglobin-1;
DE   AltName: Full=Leghemoglobin I;
OS   Pisum sativum (Garden pea).
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; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-148.
RC   STRAIN=cv. Torstai; TISSUE=Root nodule;
RX   PubMed=7378476; DOI=10.1016/0005-2795(80)90012-4;
RA   Lehtovaara P., Lappalainen A., Ellfolk N.;
RT   "The amino acid sequence of pea (Pisum sativum) leghemoglobin.";
RL   Biochim. Biophys. Acta 623:98-106(1980).
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   PIR; A02555; GPPMI.
DR   AlphaFoldDB; P02233; -.
DR   SMR; P02233; -.
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|PubMed:7378476"
FT   CHAIN           2..148
FT                   /note="Leghemoglobin-1"
FT                   /id="PRO_0000192991"
FT   BINDING         61
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         93
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   VARIANT         22
FT                   /note="P -> Q"
FT   VARIANT         24..25
FT                   /note="YS -> NA"
FT   VARIANT         26
FT                   /note="I -> T"
FT   VARIANT         26
FT                   /note="I -> V"
FT   VARIANT         32
FT                   /note="V -> I"
FT   VARIANT         94..95
FT                   /note="VQ -> AG"
SQ   SEQUENCE   148 AA;  15966 MW;  6A6A6F3EE99D4589 CRC64;
     MGFTDKQEAL VNSSSEFKQN LPGYSILFYT IVLEKAPAAK GLFSFLKDTA GVEDSPKLQA
     HAEQVFGLVR DSAAQLRTKG EVVLGNATLG AIHVQKGVTN PHFVVVKEAL LQTIKKASGN
     NWSEELNTAW EVAYDGLATA IKKAMKTA
 
 
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