Reviewed, UniProtKB/Swiss-Prot P00318 (PHAB_MASLA)

Names and origin

Protein names

Recommended name:
    Allophycocyanin beta chain

Gene names

Name:

apcB

Organism

Mastigocladus laminosus (Fischerella sp.)

Taxonomic identifier

83541 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Stigonematales › Mastigocladus

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers.
Subunit structure	Heterodimer of an alpha and a beta chain.
Subcellular location	Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note: Forms the core of the phycobilisome.
Post-translational modification	Contains one covalently linked phycocyanobilin chromophore.
Sequence similarities	Belongs to the phycobiliprotein family.

Ontologies

Keywords
Biological process	Electron transport Photosynthesis Transport
Cellular component	Membrane Phycobilisome Thylakoid
Ligand	Bile pigment Chromophore
PTM	Methylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis Inferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	phycobilisome 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 – 161

161

Allophycocyanin beta chain

PRO_0000199099

Sites

Binding site

81

1

Phycocyanobilin chromophore (covalent; via 1 link)

Amino acid modifications

Modified residue

71

1

N4-methylasparagine Ref.2 Ref.3 Ref.4

Experimental info

Sequence conflict

59 – 60

2

SL → KT AA sequence Ref.1

Sequence conflict

67

1

R → L AA sequence Ref.1

Sequence conflict

71

1

N → D AA sequence Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

161

Helix Strand Turn

Details...

Helix

4 – 13

10

Turn

14 – 16

3

Helix

21 – 46

26

Helix

48 – 59

12

Turn

60 – 62

3

Turn

64 – 66

3

Helix

75 – 98

24

Helix

102 – 107

6

Helix

112 – 119

8

Helix

123 – 160

38

Sequences

	Sequence		Length	Mass (Da)
	P00318-1 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: 18E7DD78D7178350	FASTA	161	17,374
	10 20 30 40 50 60 MQDAITAVIN SSDVQGKYLD TAALEKLKSY FSTGELRVRA ATTIAANAAA IVKEAVAKSL 70 80 90 100 110 120 LYSDITRPGG NMYTTRRYAA CIRDLDYYLR YATYAMLAGD PSILDERVLN GLKETYNSLG 130 140 150 160 VPISATVQAI QAMKEVTASL VGPDAGKEMG VYFDYICSGL S

References

[1]	"The complete amino acid sequence of both subunits of allophycocyanin, a light harvesting protein-pigment complex from the cyanobacterium Mastigocladus laminosus." Sidler W., Gysi J., Isker E., Zuber H. Hoppe-Seyler's Z. Physiol. Chem. 362:611-628(1981) [PubMed: 6792029] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Isolation and localization of N4-methylasparagine in phycobiliproteins from the cyanobacterium Mastigocladus laminosus." Ruembeli R., Suter F., Wirth M., Sidler W., Zuber H. Biol. Chem. Hoppe-Seyler 368:1401-1406(1987) [PubMed: 3122783] [Abstract] Cited for: PROTEIN SEQUENCE OF 59-82, METHYLATION AT ASN-71.
[3]	"Gamma-N-methylasparagine in phycobiliproteins from the cyanobacteria Mastigocladus laminosus and Calothrix." Ruembeli R., Suter F., Wirth M., Sidler W., Zuber H. FEBS Lett. 221:1-2(1987) Cited for: PROTEIN SEQUENCE OF 55-82, METHYLATION AT ASN-71.
[4]	"Structural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus." Reuter W., Wiegand G., Huber R., Than M.E. Proc. Natl. Acad. Sci. U.S.A. 96:1363-1368(1999) [PubMed: 9990029] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), METHYLATION AT ASN-71. Strain: PCC 7603.

Cross-references

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B33	X-ray	2.30	B/D/F/I/K/M	1-161	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR006245. ApcB.
IPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
[Graphical view]

Gene3D

G3DSA:1.10.490.20. Phycobilisome. 1 hit.

Pfam

PF00502. Phycobilisome. 1 hit.
[Graphical view]

PIRSF

PIRSF000081. Phycocyanin. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PHAB_MASLA

Accession

Primary (citable) accession number: P00318

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1991
Last modified:	December 15, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)