ID   TRHN1_CHLMO             Reviewed;         164 AA.
AC   Q08753;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Group 1 truncated hemoglobin LI637;
DE            Short=CtrHb;
DE            Short=Truncated Hb;
DE   AltName: Full=Globin LI637;
DE   Flags: Precursor;
GN   Name=LI637;
OS   Chlamydomonas moewusii (Chlamydomonas eugametos).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=UTEX 9;
RX   PubMed=8177215; DOI=10.1007/bf00280316;
RA   Couture M., Chamberland H., St Pierre B., Lafontaine J., Guertin M.;
RT   "Nuclear genes encoding chloroplast hemoglobins in the unicellular green
RT   alga Chlamydomonas eugametos.";
RL   Mol. Gen. Genet. 243:185-197(1994).
RN   [2]
RP   CHARACTERIZATION, AND MUTAGENESIS OF TYR-63.
RX   PubMed=10563822; DOI=10.1021/bi991237e;
RA   Das T.K., Couture M., Lee H.C., Peisach J., Rousseau D.L., Wittenberg B.A.,
RA   Wittenberg J.B., Guertin M.;
RT   "Identification of the ligands to the ferric heme of Chlamydomonas
RT   chloroplast hemoglobin: evidence for ligation of tyrosine-63 (B10) to the
RT   heme.";
RL   Biochemistry 38:15360-15368(1999).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN THE CYANO-MET FORM, AND SUBUNIT.
RX   PubMed=10835341; DOI=10.1093/emboj/19.11.2424;
RA   Pesce A., Couture M., Dewilde S., Guertin M., Yamauchi K., Ascenzi P.,
RA   Moens L., Bolognesi M.;
RT   "A novel two-over-two alpha-helical sandwich fold is characteristic of the
RT   truncated hemoglobin family.";
RL   EMBO J. 19:2424-2434(2000).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 44-164, AND SUBUNIT.
RX   PubMed=15016811; DOI=10.1074/jbc.m401320200;
RA   Milani M., Pesce A., Ouellet Y., Dewilde S., Friedman J., Ascenzi P.,
RA   Guertin M., Bolognesi M.;
RT   "Heme-ligand tunneling in group I truncated hemoglobins.";
RL   J. Biol. Chem. 279:21520-21525(2004).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC       Note=Binds 1 heme group per subunit.;
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10835341,
CC       ECO:0000269|PubMed:15016811}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Note=Particularly in the
CC       pyrenoid and the thylakoid region.
CC   -!- INDUCTION: By light.
CC   -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group I
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X65870; CAA46700.1; -; Genomic_DNA.
DR   EMBL; X72916; CAA51421.1; -; mRNA.
DR   PIR; S43908; S43908.
DR   PDB; 1DLY; X-ray; 1.80 A; A=1-164.
DR   PDB; 1UVX; X-ray; 2.45 A; A=44-164.
DR   PDBsum; 1DLY; -.
DR   PDBsum; 1UVX; -.
DR   AlphaFoldDB; Q08753; -.
DR   SMR; Q08753; -.
DR   EvolutionaryTrace; Q08753; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR019795; Globin_bac-like_CS.
DR   InterPro; IPR001486; Hemoglobin_trunc.
DR   Pfam; PF01152; Bac_globin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01213; GLOBIN_FAM_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Heme; Iron; Metal-binding; Oxygen transport;
KW   Plastid; Transit peptide; Transport.
FT   TRANSIT         1..22
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..164
FT                   /note="Group 1 truncated hemoglobin LI637"
FT                   /id="PRO_0000162635"
FT   BINDING         63
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="distal binding residue"
FT   BINDING         111
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT   MUTAGEN         63
FT                   /note="Y->L: Changes iron coordination."
FT                   /evidence="ECO:0000269|PubMed:10563822"
FT   HELIX           45..48
FT                   /evidence="ECO:0007829|PDB:1DLY"
FT   HELIX           51..67
FT                   /evidence="ECO:0007829|PDB:1DLY"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:1DLY"
FT   HELIX           73..76
FT                   /evidence="ECO:0007829|PDB:1DLY"
FT   HELIX           81..95
FT                   /evidence="ECO:0007829|PDB:1DLY"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:1DLY"
FT   HELIX           107..111
FT                   /evidence="ECO:0007829|PDB:1DLY"
FT   HELIX           120..136
FT                   /evidence="ECO:0007829|PDB:1DLY"
FT   HELIX           141..152
FT                   /evidence="ECO:0007829|PDB:1DLY"
FT   HELIX           155..158
FT                   /evidence="ECO:0007829|PDB:1DLY"
SQ   SEQUENCE   164 AA;  17871 MW;  26F227E4B55752AB CRC64;
     MMRTVQLRTL RPCIRAQQQP VRPSTSATAA AATAPAPARK CPSSLFAKLG GREAVEAAVD
     KFYNKIVADP TVSTYFSNTD MKVQRSKQFA FLAYALGGAS EWKGKDMRTA HKDLVPHLSD
     VHFQAVARHL SDTLTELGVP PEDITDAMAV VASTRTEVLN MPQQ