Lysyl oxidase - Pichia pastoris (Yeast)

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Q96X16 (Q96X16_PICPA) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 45. History...

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

Third-party data

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

Names and origin

Protein names

Submitted name:
Lysyl oxidase EMBL AAK49976.1

Gene names

Name:

AOC1 EMBL AAK49976.1

Organism

Pichia pastoris (Yeast) EMBL AAK49976.1

Taxonomic identifier

4922 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Komagataella

Protein attributes

Sequence length	787 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the copper/topaquinone oxidase family. RuleBase RU004199

Ontologies

Keywords
Ligand	Calcium PDB 1N9E PDB 1RKY PDB 1W7C Copper PDB 1N9E PDB 1RKY PDB 1W7C Metal-binding PDB 1N9E PDB 1RKY PDB 1W7C
Technical term	3D-structure PDB 1N9E PDB 1RKY PDB 1W7C
Gene Ontology (GO)
Biological process	amine metabolic process Inferred from electronic annotation. Source: InterPro cellular response to inorganic substance Inferred from direct assay. Source: UniProtKB
Molecular function	copper ion binding Inferred from electronic annotation. Source: InterPro diamine oxidase activity Inferred from direct assay. Source: UniProtKB primary amine oxidase activity Inferred from electronic annotation. Source: InterPro quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

478

Copper PDB 1N9E PDB 1RKY

Metal binding

528

Copper; via tele nitrogen PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

530

Copper; via tele nitrogen PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

537

Calcium 1 PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

538

Calcium 1; via carbonyl oxygen PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

539

Calcium 1 PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

580

Calcium 2 PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

673

Calcium 2; via carbonyl oxygen PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

675

Calcium 2 PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

677

Calcium 2 PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

683

Calcium 1 PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

684

Calcium 1; via carbonyl oxygen PDB 1N9E PDB 1RKY PDB 1W7C

Metal binding

694

Copper; via pros nitrogen PDB 1N9E PDB 1RKY PDB 1W7C

Amino acid modifications

Modified residue

477

2',4',5'-topaquinone PDB 1W7C

Modified residue

478

2',4',5'-topaquinone PDB 1N9E PDB 1RKY PDB 1W7C

Modified residue

479

2',4',5'-topaquinone (covalent) PDB 1W7C

Glycosylation

N-linked (GlcNAc...) PDB 1N9E PDB 1RKY PDB 1W7C

Glycosylation

104

N-linked (GlcNAc...) PDB 1N9E PDB 1RKY PDB 1W7C

Glycosylation

191

N-linked (GlcNAc...) PDB 1N9E PDB 1RKY PDB 1W7C

Glycosylation

309

N-linked (GlcNAc...) PDB 1N9E PDB 1RKY PDB 1W7C

Glycosylation

434

N-linked (GlcNAc...) PDB 1N9E PDB 1RKY PDB 1W7C

Sequences

Sequence

Length

Mass (Da)

Tools

Q96X16 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: D779E8F2BF766745
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FASTA

787

89,691

        10         20         30         40         50         60 
MRLTNLLSLT TLVALAVAVP DFYQKREAVS SKEAALLRRD ASAECVSNEN VEIEAPKTNI 

        70         80         90        100        110        120 
WTSLAKEEVQ EVLDLLHSTY NITEVTKADF FSNYVLWIET LKPNKTEALT YLDEDGDLPP 

       130        140        150        160        170        180 
RNARTVVYFG EGEEGYFEEL KVGPLPVSDE TTIEPLSFYN TNGKSKLPFE VGHLDRIKSA 

       190        200        210        220        230        240 
AKSSFLNKNL NTTIMRDVLE GLIGVPYEDM GCHSAAPQLH DPATGATVDY GTCNINTEND 

       250        260        270        280        290        300 
AENLVPTGFF FKFDMTGRDV SQWKMLEYIY NNKVYTSAEE LYEAMQKDDF VTLPKIDVDN 

       310        320        330        340        350        360 
LDWTVIQRND SAPIRHLDDR KSPRLVEPEG RRWAYDGEEE YFSWMDWGFY TSWSRDTGIS 

       370        380        390        400        410        420 
FYDITFKGER IVYELSLQEL IAEYGSDDPF NQHTFYSDIS YGVGNRFSLV PGYDCPATAG 

       430        440        450        460        470        480 
YFTTDTFEYD EFYNRTLSYC VFENQEDYSL LRHTGASYSA ITQNPTLNVR FISTIGNYDY 

       490        500        510        520        530        540 
NFLYKFFLDG TLEVSVRAAG YIQAGYWNPE TSAPYGLKIH DVLSGSFHDH VLNYKVDLDV 

       550        560        570        580        590        600 
GGTKNRASKY VMKDVDVEYP WAPGTVYNTK QIAREVLEKE DFNGINWPEN GQGILLIESA 

       610        620        630        640        650        660 
EETNSFGNPR AYNIMPGGGG VHRIVKNSRS GPETQNWARS NLFLTKHKDE ELRSSTALNT 

       670        680        690        700        710        720 
NALYDPPVNF NAFLDDESLD GEDIVAWVNL GLHHLPNSND LPNTIFSTAH ASFMLTPFNY 

       730        740        750        760        770        780 
FDSENSRDTT QQVFYTYDDE TEESNWEFYG NDWSSCGLEV PEPNFEDYTY GRGTRINKKM 


TNSDEVY

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References

[1]	"Cloning, sequence analysis, and characterization of the 'lysyl oxidase' from Pichia pastoris." Kucha J.A., Dooley D.M. J. Inorg. Biochem. 83:193-204(2001) [PubMed: 11237259] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The crystal structure of Pichia pastoris lysyl oxidase." Duff A.P., Cohen A.E., Ellis P.J., Kuchar J.A., Langley D.B., Shepard E.M., Dooley D.M., Freeman H.C., Guss J.M. Biochemistry 42:15148-15157(2003) [PubMed: 14690425] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH CALCIUM AND COPPER, TOPAQUINONE AT TYR-478, GLYCOSYLATION AT ASN-81; ASN-104; ASN-191; ASN-309 AND ASN-434.
[3]	"The 1.23 Angstrom structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link." Duff A.P., Cohen A.E., Ellis P.J., Hilmer K., Langley D.B., Dooley D.M., Freeman H.C., Guss J.M. Acta Crystallogr. D Biol. Crystallogr. 62:1073-1084(2006) [PubMed: 16929109] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS) OF 41-787 IN COMPLEX WITH CALCIUM AND COPPER, TOPAQUINONE AT ASN-477; TYR-478 AND ASP-479, GLYCOSYLATION AT ASN-81; ASN-104; ASN-191; ASN-309 AND ASN-434.
[4]	"Using xenon as a probe for dioxygen-binding sites in copper amine oxidases." Duff A.P., Trambaiolo D.M., Cohen A.E., Ellis P.J., Juda G.A., Shepard E.M., Langley D.B., Dooley D.M., Freeman H.C., Guss J.M. J. Mol. Biol. 344:599-607(2004) [PubMed: 15533431] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 41-787 IN COMPLEX WITH CALCIUM AND COPPER, TOPAQUINONE AT TYR-478, GLYCOSYLATION AT ASN-81; ASN-104; ASN-191; ASN-309 AND ASN-434.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF358434 Genomic DNA. Translation: AAK49976.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N9E	X-ray	1.65	A/B/C/D	1-787	[»]
1RKY	X-ray	1.68	A	41-787	[»]
1W7C	X-ray	1.23	A	41-787	[»]

ProteinModelPortal

Q96X16.

SMR

Q96X16. Positions 41-775.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015328. DUF1965.
[Graphical view]

Gene3D

G3DSA:3.10.450.40. CuNH_oxidase. 2 hits.
G3DSA:2.70.98.20. Lyase_8_central. 1 hit.

PANTHER

PTHR10638. CuNH_oxidase. 1 hit.

Pfam

PF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF09248. DUF1965. 1 hit.
[Graphical view]

PRINTS

PR00766. CUDAOXIDASE.

SUPFAM

SSF54416. Cu_amine_oxidase_N-reg. 2 hits.
SSF49998. CuNH_oxidase. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q96X16_PICPA

Accession

Primary (citable) accession number: Q96X16

Entry history

Integrated into UniProtKB/TrEMBL:	December 1, 2001
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information