TRHBN_SYNY3
ID TRHBN_SYNY3 Reviewed; 124 AA.
AC P73925;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Group 1 truncated hemoglobin GlbN;
DE Short=Truncated Hb;
DE Short=trHbN;
DE AltName: Full=Cyanoglobin;
DE AltName: Full=Hemoglobin;
DE Short=Hb;
DE AltName: Full=SynHb;
GN Name=glbN; OrderedLocusNames=slr2097;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP CHARACTERIZATION, AND MUTAGENESIS OF HIS-46.
RX PubMed=10903511; DOI=10.1046/j.1432-1327.2000.01531.x;
RA Couture M., Das T.K., Savard P.Y., Ouellet Y., Wittenberg J.B.,
RA Wittenberg B.A., Rousseau D.L., Guertin M.;
RT "Structural investigations of the hemoglobin of the cyanobacterium
RT Synechocystis PCC6803 reveal a unique distal heme pocket.";
RL Eur. J. Biochem. 267:4770-4780(2000).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10752621; DOI=10.1110/ps.9.3.587;
RA Scott N.L., Lecomte J.T.J.;
RT "Cloning, expression, purification, and preliminary characterization of a
RT putative hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803.";
RL Protein Sci. 9:587-597(2000).
RN [4]
RP COVALENT HEME ATTACHMENT.
RX PubMed=12121092; DOI=10.1021/ja026569c;
RA Vu B.C., Jones A.D., Lecomte J.T.J.;
RT "Novel histidine-heme covalent linkage in a hemoglobin.";
RL J. Am. Chem. Soc. 124:8544-8545(2002).
RN [5]
RP STRUCTURE BY NMR OF 2-124 IN THE LOW-SPIN FE(3+) STATE.
RX PubMed=12470956; DOI=10.1016/s0022-2836(02)01093-8;
RA Falzone C.J., Christie Vu B., Scott N.L., Lecomte J.T.;
RT "The solution structure of the recombinant hemoglobin from the
RT cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state.";
RL J. Mol. Biol. 324:1015-1029(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-124, AND SUBUNIT.
RX PubMed=14736872; DOI=10.1074/jbc.m313707200;
RA Hoy J.A., Kundu S., Trent J.T. III, Ramaswamy S., Hargrove M.S.;
RT "The crystal structure of Synechocystis hemoglobin with a covalent heme
RT linkage.";
RL J. Biol. Chem. 279:16535-16542(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN CYANIDE AND AZIDE-BOUND FORMS.
RX PubMed=15289104; DOI=10.1016/j.jmb.2004.05.070;
RA Trent J.T. III, Kundu S., Hoy J.A., Hargrove M.S.;
RT "Crystallographic analysis of synechocystis cyanoglobin reveals the
RT structural changes accompanying ligand binding in a hexacoordinate
RT hemoglobin.";
RL J. Mol. Biol. 341:1097-1108(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-124 IN THE FE(2+) AND FE(3+)
RP FORMS, AND MUTAGENESIS OF HIS-117.
RX PubMed=17242429; DOI=10.1110/ps.062572607;
RA Hoy J.A., Smagghe B.J., Halder P., Hargrove M.S.;
RT "Covalent heme attachment in Synechocystis hemoglobin is required to
RT prevent ferrous heme dissociation.";
RL Protein Sci. 16:250-260(2007).
CC -!- FUNCTION: Forms a very stable complex with oxygen. The oxygen
CC dissociation rate is 0.011 sec(-1).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14736872}.
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group I
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000022; BAA17991.1; -; Genomic_DNA.
DR PIR; S75129; S75129.
DR PDB; 1MWB; NMR; -; A=2-124.
DR PDB; 1RTX; X-ray; 1.80 A; A=2-124.
DR PDB; 1S69; X-ray; 1.68 A; A=1-124.
DR PDB; 1S6A; X-ray; 1.69 A; A=1-124.
DR PDB; 2HZ1; X-ray; 1.80 A; A=2-124.
DR PDB; 2HZ2; X-ray; 2.00 A; A=2-124.
DR PDB; 2HZ3; X-ray; 1.90 A; A=2-124.
DR PDBsum; 1MWB; -.
DR PDBsum; 1RTX; -.
DR PDBsum; 1S69; -.
DR PDBsum; 1S6A; -.
DR PDBsum; 2HZ1; -.
DR PDBsum; 2HZ2; -.
DR PDBsum; 2HZ3; -.
DR AlphaFoldDB; P73925; -.
DR SMR; P73925; -.
DR STRING; 1148.1653074; -.
DR PaxDb; P73925; -.
DR EnsemblBacteria; BAA17991; BAA17991; BAA17991.
DR KEGG; syn:slr2097; -.
DR eggNOG; COG2346; Bacteria.
DR InParanoid; P73925; -.
DR OMA; HQKAFLT; -.
DR PhylomeDB; P73925; -.
DR BioCyc; MetaCyc:MON-19373; -.
DR EvolutionaryTrace; P73925; -.
DR Proteomes; UP000001425; Chromosome.
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:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
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 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 InterPro; IPR016339; Hemoglobin_trunc_I.
DR Pfam; PF01152; Bac_globin; 1.
DR PIRSF; PIRSF002030; Globin_Protozoa/Cyanobacteria; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01213; GLOBIN_FAM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT CHAIN 1..124
FT /note="Group 1 truncated hemoglobin GlbN"
FT /id="PRO_0000162646"
FT BINDING 46
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 70
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 BINDING 117
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT MUTAGEN 46
FT /note="H->A: Changes iron coordination."
FT /evidence="ECO:0000269|PubMed:10903511"
FT MUTAGEN 117
FT /note="H->A: Increases heme dissociation from the Fe(2+)
FT hexacoordinate complex."
FT /evidence="ECO:0000269|PubMed:17242429"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:1S69"
FT HELIX 10..26
FT /evidence="ECO:0007829|PDB:1S69"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1S69"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:1S69"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:1S69"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1S69"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:1S69"
FT HELIX 81..98
FT /evidence="ECO:0007829|PDB:1S69"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:1S69"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:1S69"
SQ SEQUENCE 124 AA; 13868 MW; 8F53B809B8358844 CRC64;
MSTLYEKLGG TTAVDLAVDK FYERVLQDDR IKHFFADVDM AKQRAHQKAF LTYAFGGTDK
YDGRYMREAH KELVENHGLN GEHFDAVAED LLATLKEMGV PEDLIAEVAA VAGAPAHKRD
VLNQ
