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Protein

Group 1 truncated hemoglobin GlbN

Gene

glbN

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Forms a very stable complex with oxygen. The oxygen dissociation rate is 0.011 s(-1).

Cofactori

hemeNote: Binds 1 heme group per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi46 – 461Iron (heme distal ligand)
Metal bindingi70 – 701Iron (heme proximal ligand)
Binding sitei117 – 1171Heme (covalent; via tele nitrogen)

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Group 1 truncated hemoglobin GlbN
Short name:
Truncated Hb
Short name:
trHbN
Alternative name(s):
Cyanoglobin
Hemoglobin
Short name:
Hb
SynHb
Gene namesi
Name:glbN
Ordered Locus Names:slr2097
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461H → A: Changes iron coordination. 1 Publication
Mutagenesisi117 – 1171H → A: Increases heme dissociation from the Fe(2+) hexacoordinate complex. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 124124Group 1 truncated hemoglobin GlbNPRO_0000162646Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
124
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 85Combined sources
Helixi10 – 2617Combined sources
Turni29 – 313Combined sources
Helixi32 – 354Combined sources
Helixi40 – 5415Combined sources
Beta strandi57 – 593Combined sources
Helixi66 – 7712Combined sources
Helixi81 – 9818Combined sources
Helixi102 – 11312Combined sources
Helixi115 – 1217Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MWBNMR-A2-124[»]
1RTXX-ray1.80A2-124[»]
1S69X-ray1.68A1-124[»]
1S6AX-ray1.69A1-124[»]
2HZ1X-ray1.80A2-124[»]
2HZ2X-ray2.00A2-124[»]
2HZ3X-ray1.90A2-124[»]
ProteinModelPortaliP73925.
SMRiP73925. Positions 2-124.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP73925.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000262697.
InParanoidiP73925.
KOiK06886.
OMAiISHFFED.
OrthoDBiEOG62K1ZS.
PhylomeDBiP73925.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR019795. Globin_bac-like_CS.
IPR001486. Hemoglobin_trunc.
IPR016339. Hemoglobin_trunc_I.
[Graphical view]
PfamiPF01152. Bac_globin. 1 hit.
[Graphical view]
PIRSFiPIRSF002030. Globin_Protozoa/Cyanobacteria. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01213. GLOBIN_FAM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P73925-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLYEKLGG TTAVDLAVDK FYERVLQDDR IKHFFADVDM AKQRAHQKAF
60 70 80 90 100
LTYAFGGTDK YDGRYMREAH KELVENHGLN GEHFDAVAED LLATLKEMGV
110 120
PEDLIAEVAA VAGAPAHKRD VLNQ
Length:124
Mass (Da):13,868
Last modified:February 1, 1997 - v1
Checksum:i8F53B809B8358844
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17991.1.
PIRiS75129.

Genome annotation databases

EnsemblBacteriaiBAA17991; BAA17991; BAA17991.
KEGGisyn:slr2097.
PATRICi23839988. VBISynSp132158_1554.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17991.1.
PIRiS75129.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MWBNMR-A2-124[»]
1RTXX-ray1.80A2-124[»]
1S69X-ray1.68A1-124[»]
1S6AX-ray1.69A1-124[»]
2HZ1X-ray1.80A2-124[»]
2HZ2X-ray2.00A2-124[»]
2HZ3X-ray1.90A2-124[»]
ProteinModelPortaliP73925.
SMRiP73925. Positions 2-124.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA17991; BAA17991; BAA17991.
KEGGisyn:slr2097.
PATRICi23839988. VBISynSp132158_1554.

Phylogenomic databases

HOGENOMiHOG000262697.
InParanoidiP73925.
KOiK06886.
OMAiISHFFED.
OrthoDBiEOG62K1ZS.
PhylomeDBiP73925.

Miscellaneous databases

EvolutionaryTraceiP73925.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR019795. Globin_bac-like_CS.
IPR001486. Hemoglobin_trunc.
IPR016339. Hemoglobin_trunc_I.
[Graphical view]
PfamiPF01152. Bac_globin. 1 hit.
[Graphical view]
PIRSFiPIRSF002030. Globin_Protozoa/Cyanobacteria. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01213. GLOBIN_FAM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.
  2. "Structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC6803 reveal a unique distal heme pocket."
    Couture M., Das T.K., Savard P.Y., Ouellet Y., Wittenberg J.B., Wittenberg B.A., Rousseau D.L., Guertin M.
    Eur. J. Biochem. 267:4770-4780(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-46.
  3. "Cloning, expression, purification, and preliminary characterization of a putative hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803."
    Scott N.L., Lecomte J.T.J.
    Protein Sci. 9:587-597(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "Novel histidine-heme covalent linkage in a hemoglobin."
    Vu B.C., Jones A.D., Lecomte J.T.J.
    J. Am. Chem. Soc. 124:8544-8545(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: COVALENT HEME ATTACHMENT.
  5. "The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state."
    Falzone C.J., Christie Vu B., Scott N.L., Lecomte J.T.
    J. Mol. Biol. 324:1015-1029(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-124 IN THE LOW-SPIN FE(3+) STATE.
  6. "The crystal structure of Synechocystis hemoglobin with a covalent heme linkage."
    Hoy J.A., Kundu S., Trent J.T. III, Ramaswamy S., Hargrove M.S.
    J. Biol. Chem. 279:16535-16542(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-124, SUBUNIT.
  7. "Crystallographic analysis of synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin."
    Trent J.T. III, Kundu S., Hoy J.A., Hargrove M.S.
    J. Mol. Biol. 341:1097-1108(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN CYANIDE AND AZIDE-BOUND FORMS.
  8. "Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation."
    Hoy J.A., Smagghe B.J., Halder P., Hargrove M.S.
    Protein Sci. 16:250-260(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-124 IN THE FE(2+) AND FE(3+) FORMS, MUTAGENESIS OF HIS-117.

Entry informationi

Entry nameiTRHBN_SYNY3
AccessioniPrimary (citable) accession number: P73925
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: February 1, 1997
Last modified: March 16, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.