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Protein

O-aminophenol oxidase

Gene

phsA

Organism
Streptomyces antibioticus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Could be involved in the spore pigmentation and melanin production. Catalyzes the oxidative coupling of 2-aminophenols to form the 2-aminophenoxazinone chromophore. 2-aminophenoxazinone synthesis proceeds via a sequence of three consecutive 2-electron aminophenol oxidations. First, the o-aminophenol is oxidized by two electrons to the quinone imine, which then conjugates to a second o-aminophenol molecule while still bound to the enzyme. This product is further oxidized by two electrons to give rise to the p-quinone imine. The last two steps of the reaction, another conjugation to generate the tricyclic structure and a final two-electron oxidation to yield the 2-aminophenoxazinone product, are thought to be non-enzymatic. It can also uuse 3-hydroxyanthranilic acid (HAA), 4-methyl-3-hydroxyanthranilic acid (MHA), 3,4-dihydroxy-L-phenylalanine (L-DOPA), ferrocyanide and thiophenol as substrates.1 Publication3 Publications

Catalytic activityi

4 2-aminophenol + 3 O2 = 2 2-aminophenoxazin-3-one + 6 H2O.2 Publications

Cofactori

Cu2+1 Publication2 PublicationsNote: Binds 5 copper ions per monomer.1 Publication2 Publications

Kineticsi

  1. KM=207 µM for dioxygen1 Publication
  2. KM=240 µM for MHA1 Publication
  3. KM=400 µM for HAA1 Publication
  4. KM=400 µM for thiophenol1 Publication
  5. KM=500 µM for L-DOPA1 Publication
  6. KM=500 µM for 2-aminophenol1 Publication
  7. KM=710 µM for ferrocyanide1 Publication
  1. Vmax=8.6 µmol/min/mg enzyme toward 2-aminophenol1 Publication
  2. Vmax=36.6 µmol/min/mg enzyme toward dioxygen1 Publication

pH dependencei

Optimum pH is 5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi162Copper 1; type 21 Publication1
Metal bindingi164Copper 2; type 31 Publication1
Metal bindingi202Copper 2; type 31 Publication1
Metal bindingi204Copper 3; type 31 Publication1
Metal bindingi435Copper 4; type 21 Publication1
Metal bindingi439Copper 4; type 21 Publication1
Metal bindingi441Copper 4; type 21 Publication1
Metal bindingi525Copper 5; type 11 Publication1
Metal bindingi528Copper 1; type 21 Publication1
Metal bindingi530Copper 3; type 31 Publication1
Metal bindingi603Copper 3; type 31 Publication1
Metal bindingi604Copper 5; type 11 Publication1
Metal bindingi605Copper 2; type 31 Publication1
Metal bindingi609Copper 5; type 11 Publication1
Metal bindingi614Copper 5; type 11 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19511.

Names & Taxonomyi

Protein namesi
Recommended name:
O-aminophenol oxidase1 Publication (EC:1.10.3.42 Publications)
Alternative name(s):
Phenoxazinone synthase1 Publication
Short name:
PHS1 Publication
Gene namesi
Name:phsA1 Publication
OrganismiStreptomyces antibioticus
Taxonomic identifieri1890 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000855832 – 643O-aminophenol oxidaseAdd BLAST642

Interactioni

Subunit structurei

Homodimer (small form) or homohexamer (large form).3 Publications

Structurei

Secondary structure

1643
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi66 – 75Combined sources10
Beta strandi84 – 89Combined sources6
Beta strandi92 – 94Combined sources3
Beta strandi97 – 101Combined sources5
Beta strandi106 – 112Combined sources7
Beta strandi121 – 127Combined sources7
Helixi137 – 139Combined sources3
Helixi150 – 153Combined sources4
Beta strandi161 – 164Combined sources4
Turni170 – 172Combined sources3
Helixi176 – 178Combined sources3
Beta strandi185 – 190Combined sources6
Beta strandi196 – 203Combined sources8
Turni206 – 208Combined sources3
Helixi209 – 212Combined sources4
Turni213 – 216Combined sources4
Beta strandi218 – 224Combined sources7
Helixi226 – 229Combined sources4
Turni230 – 232Combined sources3
Helixi236 – 238Combined sources3
Beta strandi239 – 247Combined sources9
Beta strandi249 – 251Combined sources3
Beta strandi257 – 271Combined sources15
Beta strandi273 – 276Combined sources4
Beta strandi286 – 290Combined sources5
Beta strandi293 – 295Combined sources3
Beta strandi297 – 311Combined sources15
Beta strandi318 – 323Combined sources6
Beta strandi333 – 339Combined sources7
Beta strandi342 – 350Combined sources9
Beta strandi352 – 361Combined sources10
Beta strandi366 – 372Combined sources7
Beta strandi380 – 385Combined sources6
Helixi397 – 399Combined sources3
Beta strandi405 – 412Combined sources8
Beta strandi440 – 447Combined sources8
Turni452 – 456Combined sources5
Beta strandi459 – 465Combined sources7
Beta strandi479 – 483Combined sources5
Beta strandi489 – 496Combined sources8
Beta strandi505 – 508Combined sources4
Beta strandi512 – 519Combined sources8
Beta strandi521 – 523Combined sources3
Beta strandi525 – 531Combined sources7
Beta strandi533 – 543Combined sources11
Turni549 – 552Combined sources4
Beta strandi553 – 556Combined sources4
Beta strandi558 – 565Combined sources8
Beta strandi576 – 581Combined sources6
Beta strandi583 – 592Combined sources10
Beta strandi598 – 606Combined sources9
Helixi607 – 611Combined sources5
Beta strandi615 – 621Combined sources7
Helixi623 – 626Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GYRX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L32-643[»]
ProteinModelPortaliQ53692.
SMRiQ53692.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini87 – 224Plastocyanin-like 1Sequence analysisAdd BLAST138
Domaini494 – 621Plastocyanin-like 2Sequence analysisAdd BLAST128

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 2 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

KOiK20219.

Family and domain databases

Gene3Di2.60.40.420. 4 hits.
InterProiIPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q53692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDMIEQSDD RIDPIDGVLA DGVLADDVLA KEREQAPAPG ELTPFAAPLT
60 70 80 90 100
VPPVLRPASD EVTRETEIAL RPTWVRLHPQ LPPTLMWGYD GQVPGPTIEV
110 120 130 140 150
RRGQRVRIAW TNRIPKGSEY PVTSVEVPLG PPGTPAPNTE PGRGGVEPNK
160 170 180 190 200
DVAALPAWSV THLHGAQTGG GNDGWADNAV GFGDAQLSEY PNDHQATQWW
210 220 230 240 250
YHDHAMNITR WNVMAGLYGT YLVRDDEEDA LGLPSGDREI PLLIADRNLD
260 270 280 290 300
TDEDGRLNGR LLHKTVIVQQ SNPETGKPVS IPFFGPYTTV NGRIWPYADV
310 320 330 340 350
DDGWYRLRLV NASNARIYNL VLIDEDDRPV PGVVHQIGSD GGLLPRPVPV
360 370 380 390 400
DFDDTLPVLS AAPAERFDLL VDFRALGGRR LRLVDKGPGA PAGTPDPLGG
410 420 430 440 450
VRYPEVMEFR VRETCEEDSF ALPEVLSGSF RRMSHDIPHG HRLIVLTPPG
460 470 480 490 500
TKGSGGHPEI WEMAEVEDPA DVQVPAEGVI QVTGADGRTK TYRRTAATFN
510 520 530 540 550
DGLGFTIGEG THEQWTFLNL SPILHPMHIH LADFQVLGRD AYDASGFDLA
560 570 580 590 600
LGGTRTPVRL DPDTPVPLAP NELGHKDVFQ VPGPQGLRVM GKFDGAYGRF
610 620 630 640
MYHCHLLEHE DMGMMRPFVV MPPEALKFDH GGAHGGHGEG HTG
Length:643
Mass (Da):70,245
Last modified:January 23, 2007 - v3
Checksum:iFB6D9208221BDAB8
GO

Sequence cautioni

The sequence AAA86668 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04283 Unassigned DNA. Translation: AAA86668.1. Different initiation.

Genome annotation databases

KEGGiag:AAA86668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04283 Unassigned DNA. Translation: AAA86668.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GYRX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L32-643[»]
ProteinModelPortaliQ53692.
SMRiQ53692.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA86668.

Phylogenomic databases

KOiK20219.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19511.

Miscellaneous databases

EvolutionaryTraceiQ53692.

Family and domain databases

Gene3Di2.60.40.420. 4 hits.
InterProiIPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPHSA_STRAT
AccessioniPrimary (citable) accession number: Q53692
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.