P73925 (TRHBN_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Group 1 truncated hemoglobin GlbN
Short name=Truncated Hb
Short name=trHbN

Alternative name(s):
Cyanoglobin
Hemoglobin
Short name=Hb
SynHb

Gene names

Name:	glbN
Ordered Locus Names:	slr2097

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › Synechocystis sp. PCC 6803

Protein attributes

Sequence length	124 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Forms a very stable complex with oxygen. The oxygen dissociation rate is 0.011 s(-1).
Cofactor	Binds 1 heme group per subunit.
Subunit structure	Monomer. Ref.6
Sequence similarities	Belongs to the truncated hemoglobin family. Group I subfamily.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Ligand	Heme Iron Metal-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 124

124

Group 1 truncated hemoglobin GlbN

PRO_0000162646

Sites

Metal binding

46

1

Iron (heme distal ligand)

Metal binding

70

1

Iron (heme proximal ligand)

Binding site

117

1

Heme (covalent; via tele nitrogen)

Experimental info

Mutagenesis

46

1

H → A: Changes iron coordination. Ref.2

Mutagenesis

117

1

H → A: Increases heme dissociation from the Fe(2+) hexacoordinate complex. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

124

Helix Strand Turn

Details...

Helix

4 – 8

5

Helix

10 – 26

17

Turn

29 – 31

3

Helix

32 – 35

4

Helix

40 – 54

15

Beta strand

57 – 59

3

Helix

66 – 77

12

Helix

81 – 98

18

Helix

102 – 113

12

Helix

115 – 121

7

Sequences

	Sequence		Length	Mass (Da)
	P73925 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 8F53B809B8358844	FASTA	124	13,868
	10 20 30 40 50 60 MSTLYEKLGG TTAVDLAVDK FYERVLQDDR IKHFFADVDM AKQRAHQKAF LTYAFGGTDK 70 80 90 100 110 120 YDGRYMREAH KELVENHGLN GEHFDAVAED LLATLKEMGV PEDLIAEVAA VAGAPAHKRD VLNQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000022 Genomic DNA. Translation: BAA17991.1.

PIR

S75129.

RefSeq

NP_441311.1. NC_000911.1.
YP_005651368.1. NC_017277.1.
YP_007451193.1. NC_020286.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MWB	NMR	-	A	2-124	[»]
1RTX	X-ray	1.80	A	2-124	[»]
1S69	X-ray	1.68	A	1-124	[»]
1S6A	X-ray	1.69	A	1-124	[»]
2HZ1	X-ray	1.80	A	2-124	[»]
2HZ2	X-ray	2.00	A	2-124	[»]
2HZ3	X-ray	1.90	A	2-124	[»]

ProteinModelPortal

P73925.

SMR

P73925. Positions 2-124.

ModBase

Search...

Protein-protein interaction databases

STRING

1148.slr2097.

Proteomic databases

PaxDb

P73925.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAA17991; BAA17991; BAA17991.

GeneID

12255787.
14616850.
954656.

KEGG

syn:slr2097.
syy:SYNGTS_1415.

PATRIC

23839988. VBISynSp132158_1554.

Phylogenomic databases

eggNOG

COG2346.

HOGENOM

HOG000262697.

KO

K06886.

OMA

RGLNDSH.

ProtClustDB

CLSK893071.

Family and domain databases

Gene3D

1.10.490.10. 1 hit.

InterPro

IPR009050. Globin-like.
IPR019795. Globin_bac-like_CS.
IPR012292. Globin_dom.
IPR001486. Globin_trunc_bac-like.
IPR016339. Globin_trunc_bac-like_HbN/cyan.
[Graphical view]

Pfam

PF01152. Bac_globin. 1 hit.
[Graphical view]

PIRSF

PIRSF002030. Globin_Protozoa/Cyanobacteria. 1 hit.

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01213. GLOBIN_FAM_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P73925.

Entry information

Entry name

TRHBN_SYNY3

Accession

Primary (citable) accession number: P73925

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program