Amicyanin precursor - Paracoccus denitrificans

Contribute

Send feedback

Read comments (?) or add your own

P22364 (AMCY_PARDE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Amicyanin

Gene names

Name:	mauC
Synonyms:	ami

Organism

Paracoccus denitrificans

Taxonomic identifier

266 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length	131 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
Cofactor	Binds 1 copper ion per subunit.
Pathway	One-carbon metabolism; methylamine degradation.
Subcellular location	Periplasm.
Sequence similarities	Contains 1 plastocyanin-like domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Ligand	Copper Metal-binding
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

Ref.2

Chain

27 – 131

105

Amicyanin

PRO_0000002844

Regions

Domain

27 – 131

105

Plastocyanin-like

Sites

Metal binding

Copper

Metal binding

118

Copper

Metal binding

121

Copper

Metal binding

124

Copper

Secondary structure

131

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P22364 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: F7352A865FD089DA
Show »

FASTA

131

13,983

        10         20         30         40         50         60 
MISATKIRSC LAACVLAAFG ATGALADKAT IPSESPFAAA EVADGAIVVD IAKMKYETPE 

        70         80         90        100        110        120 
LHVKVGDTVT WINREAMPHN VHFVAGVLGE AALKGPMMKK EQAYSLTFTE AGTYDYHCTP 

       130 
HPFMRGKVVV E

« Hide

References

[1]	"Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation." van Spanning R.J.M., Wansell C.W., Reijnders W.N.M., Oltmann L.F., Stouthamer A.H. FEBS Lett. 275:217-220(1990) [PubMed: 2261991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 19367 / NBRC 13301 / NCIMB 8944 / NRRL B-3785.
[2]	"Properties of Paracoccus denitrificans amicyanin." Husain M., Davidson V.L. Biochemistry 25:2431-2436(1986) [PubMed: 3718960] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-36.
[3]	"Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin." Chen L., Durley R., Poliks B.J., Hamada K., Chen Z., Mathews F.S., Davidson V.L., Satow Y., Huizinga E.G., Vellieux F.M.D., Hol W.G.J. Biochemistry 31:4959-4964(1992) [PubMed: 1599920] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH MADH.
[4]	"Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i." Chen L., Durley R., Mathews F.S., Davidson V.L. Science 264:86-90(1994) [PubMed: 8140419] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[5]	"X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31-A resolution." Cunane L.M., Chen Z.-W., Durley R.C.E., Mathews F.S. Acta Crystallogr. D 52:676-686(1996) [PubMed: 15299631] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS).
[6]	"Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin." Zhu Z., Cunane L.M., Chen Z.-W., Durley R.C.E., Mathews F.S., Davidson V.L. Biochemistry 37:17128-17136(1998) [PubMed: 9860825] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), COPPER-BINDING SITES HIS-79; CYS-118; HIS-121 AND MET-124.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X55665 Genomic DNA. Translation: CAA39199.1.

PIR

A24407.
S12972.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AAC	X-ray	1.31	A	27-131	[»]
1AAJ	X-ray	1.80	A	27-131	[»]
1AAN	X-ray	2.00	A	27-131	[»]
1BXA	X-ray	1.30	A	27-131	[»]
1MDA	X-ray	2.50	A/B	29-131	[»]
1MG2	X-ray	2.25	C/G/K/O	27-131	[»]
1MG3	X-ray	2.40	C/G/K/O	27-131	[»]
1SF3	X-ray	1.05	A	27-131	[»]
1SF5	X-ray	1.10	A	27-131	[»]
1SFD	X-ray	0.99	A/B	27-131	[»]
1SFH	X-ray	1.05	A/B	27-131	[»]
1T5K	X-ray	1.40	A/B/C/D	27-131	[»]
2GB2	X-ray	1.25	A	27-131	[»]
2GBA	X-ray	0.92	A	27-131	[»]
2GC4	X-ray	1.90	C/G/K/O	27-131	[»]
2GC7	X-ray	1.90	C/G/K/O	27-131	[»]
2IDQ	X-ray	0.90	A	27-131	[»]
2IDS	X-ray	1.00	A	27-131	[»]
2IDT	X-ray	1.00	A	27-131	[»]
2IDU	X-ray	0.95	A	27-131	[»]
2J55	X-ray	2.15	A/B	27-131	[»]
2J56	X-ray	2.10	A/B	27-131	[»]
2J57	X-ray	2.25	A/B/C/D	27-131	[»]
2MTA	X-ray	2.40	A	27-131	[»]
2OV0	X-ray	0.75	A	27-131	[»]
2QDV	X-ray	0.89	A	27-131	[»]
2QDW	X-ray	0.92	A	27-131	[»]
2RAC	X-ray	1.30	A	27-131	[»]
3IE9	X-ray	2.10	A	27-131	[»]
3IEA	X-ray	2.20	A	27-131	[»]
3L45	Other	1.80	A	27-131	[»]
3PLY	X-ray	2.20	A/B/C/D	27-131	[»]
3RYM	X-ray	1.70	A/B/C/D	27-131	[»]

ProteinModelPortal

P22364.

SMR

P22364. Positions 27-131.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22364. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002386. Amicyanin.
IPR013475. Amicyanin_precur.
IPR000923. BlueCu_1.
IPR001235. Copper_blue.
IPR008972. Cupredoxin.
[Graphical view]

Gene3D

G3DSA:2.60.40.420. Cupredoxin. 1 hit.

Pfam

PF00127. Copper-bind. 1 hit.
[Graphical view]

PRINTS

PR00155. AMICYANIN.
PR00156. COPPERBLUE.

SUPFAM

SSF49503. Cupredoxin. 1 hit.

TIGRFAMs

TIGR02657. Amicyanin. 1 hit.

PROSITE

PS00196. COPPER_BLUE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AMCY_PARDE

Accession

Primary (citable) accession number: P22364

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	January 25, 2012
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents