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Database: UniProt
Entry: A8JAR4_CHLRE
LinkDB: A8JAR4_CHLRE
Original site: A8JAR4_CHLRE 
ID   A8JAR4_CHLRE            Unreviewed;       136 AA.
AC   A8JAR4;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Putative truncated hemoglobin {ECO:0000313|EMBL:ABW88998.1};
DE   SubName: Full=Truncated hemoglobin 1 {ECO:0000313|EMBL:AGM75734.1};
GN   Name=THB1 {ECO:0000313|EMBL:AGM75734.1};
GN   ORFNames=CHLRE_14g615400v5 {ECO:0000313|EMBL:PNW73013.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW73013.1, ECO:0000313|Proteomes:UP000006906};
RN   [1] {ECO:0000313|EMBL:PNW73013.1, ECO:0000313|Proteomes:UP000006906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906}, and CC-503 cw92 mt+
RC   {ECO:0000313|EMBL:PNW73013.1};
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
RN   [2] {ECO:0000313|EMBL:ABW88998.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kateriya S., Kundu S.;
RT   "Putative Truncated Hemoglobin from Chlamydomonas reinhardtii.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AGM75734.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=704 {ECO:0000313|EMBL:AGM75734.1};
RA   Sanz-Luque E., Ocana-Calahorro F., Galvan A., Fernandez E.;
RT   "A truncated hemoglobin regulated by the nitrogen source modulates nitric
RT   oxide bioactivity in Chlamydomonas reinhardtii.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0007829|PDB:4XDI}
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 2-136 IN COMPLEX WITH HEME B.
RX   PubMed=26057801; DOI=10.1107/S2053230X15006949;
RA   Rice S.L., Boucher L.E., Schlessman J.L., Preimesberger M.R., Bosch J.,
RA   Lecomte J.T.;
RT   "Structure of Chlamydomonas reinhardtii THB1, a group 1 truncated
RT   hemoglobin with a rare histidine-lysine heme ligation.";
RL   Acta Crystallogr. F Struct. Biol. Commun. 71:718-725(2015).
RN   [5] {ECO:0000313|EMBL:PNW73013.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CC-503 cw92 mt+ {ECO:0000313|EMBL:PNW73013.1};
RG   Chlamydomonas Annotation Team;
RG   JGI Annotation Team;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Grigoriev I.V., Rokhsar D.S.;
RT   "WGS assembly of Chlamydomonas reinhardtii.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0007829|PDB:6CII}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-136 IN COMPLEX WITH HEME B.
RX   DOI=10.1016/j.jinorgbio.2021.111437;
RA   Martinez J.E., Schlessman J.L., Lecomte J.T.J.;
RT   "Control of distal lysine coordination in a monomeric hemoglobin: A role
RT   for heme peripheral interactions.";
RL   J. Inorg. Biochem. 219:111437-111430(2021).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR002030-1};
CC       Note=Binds 1 heme group per subunit. {ECO:0000256|PIRSR:PIRSR002030-1};
CC   -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group I
CC       subfamily. {ECO:0000256|ARBA:ARBA00009660}.
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DR   EMBL; EU095254; ABW88998.1; -; mRNA.
DR   EMBL; KC992719; AGM75734.1; -; mRNA.
DR   EMBL; CM008975; PNW73013.1; -; Genomic_DNA.
DR   RefSeq; XP_001699005.1; XM_001698953.1.
DR   PDB; 4XDI; X-ray; 1.89 A; A/B=2-136.
DR   PDB; 6CII; X-ray; 1.70 A; A=2-136.
DR   PDBsum; 4XDI; -.
DR   PDBsum; 6CII; -.
DR   STRING; 3055.A8JAR4; -.
DR   PaxDb; 3055-EDO99059; -.
DR   EnsemblPlants; PNW73013; PNW73013; CHLRE_14g615400v5.
DR   GeneID; 5724558; -.
DR   Gramene; PNW73013; PNW73013; CHLRE_14g615400v5.
DR   KEGG; cre:CHLRE_14g615400v5; -.
DR   eggNOG; ENOG502S7S6; Eukaryota.
DR   HOGENOM; CLU_103526_2_1_1; -.
DR   OMA; HQKAFLT; -.
DR   OrthoDB; 313491at2759; -.
DR   Proteomes; UP000006906; Chromosome 14.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   CDD; cd00454; TrHb1_N; 1.
DR   Gene3D; 1.10.490.10; Globins; 1.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR001486; Hemoglobin_trunc.
DR   InterPro; IPR016339; Hemoglobin_trunc_I.
DR   Pfam; PF01152; Bac_globin; 1.
DR   PIRSF; PIRSF002030; Globin_Protozoa/Cyanobacteria; 1.
DR   SUPFAM; SSF46458; Globin-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4XDI, ECO:0007829|PDB:6CII};
KW   Heme {ECO:0000256|PIRSR:PIRSR002030-1, ECO:0007829|PDB:4XDI};
KW   Iron {ECO:0000256|PIRSR:PIRSR002030-1, ECO:0007829|PDB:4XDI};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR002030-1, ECO:0007829|PDB:4XDI};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006906}.
FT   BINDING         49
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4XDI"
FT   BINDING         52
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4XDI"
FT   BINDING         53
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:6CII"
FT   BINDING         53
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1"
FT                   /ligand_note="covalent"
FT                   /evidence="ECO:0007829|PDB:4XDI"
FT   BINDING         71
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:6CII"
FT   BINDING         77
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:6CII"
FT   BINDING         77
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:4XDI"
FT   BINDING         77
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                   /evidence="ECO:0000256|PIRSR:PIRSR002030-1"
FT   BINDING         79
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:6CII"
SQ   SEQUENCE   136 AA;  14696 MW;  A708BE9124635D2E CRC64;
     MAADTAPADS LYSRMGGEAA VEKAVDVFYE RIVADPQLAP FFANVDMKKQ RRKQVAFMTY
     VFGGSGAYEG RDLGASHRRL IREQGMNHHH FDLVAAHLDS TLQELGVAQE LKAEAMAIVA
     SARPLIFGTG EAGAAN
//
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