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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi162 – 1621Copper 1; type 21 Publication
Metal bindingi164 – 1641Copper 2; type 31 Publication
Metal bindingi202 – 2021Copper 2; type 31 Publication
Metal bindingi204 – 2041Copper 3; type 31 Publication
Metal bindingi435 – 4351Copper 4; type 21 Publication
Metal bindingi439 – 4391Copper 4; type 21 Publication
Metal bindingi441 – 4411Copper 4; type 21 Publication
Metal bindingi525 – 5251Copper 5; type 11 Publication
Metal bindingi528 – 5281Copper 1; type 21 Publication
Metal bindingi530 – 5301Copper 3; type 31 Publication
Metal bindingi603 – 6031Copper 3; type 31 Publication
Metal bindingi604 – 6041Copper 5; type 11 Publication
Metal bindingi605 – 6051Copper 2; type 31 Publication
Metal bindingi609 – 6091Copper 5; type 11 Publication
Metal bindingi614 – 6141Copper 5; type 11 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Copper, Metal-binding

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 643642O-aminophenol oxidasePRO_0000085583Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi66 – 7510Combined sources
Beta strandi84 – 896Combined sources
Beta strandi92 – 943Combined sources
Beta strandi97 – 1015Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi121 – 1277Combined sources
Helixi137 – 1393Combined sources
Helixi150 – 1534Combined sources
Beta strandi161 – 1644Combined sources
Turni170 – 1723Combined sources
Helixi176 – 1783Combined sources
Beta strandi185 – 1906Combined sources
Beta strandi196 – 2038Combined sources
Turni206 – 2083Combined sources
Helixi209 – 2124Combined sources
Turni213 – 2164Combined sources
Beta strandi218 – 2247Combined sources
Helixi226 – 2294Combined sources
Turni230 – 2323Combined sources
Helixi236 – 2383Combined sources
Beta strandi239 – 2479Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi257 – 27115Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi286 – 2905Combined sources
Beta strandi293 – 2953Combined sources
Beta strandi297 – 31115Combined sources
Beta strandi318 – 3236Combined sources
Beta strandi333 – 3397Combined sources
Beta strandi342 – 3509Combined sources
Beta strandi352 – 36110Combined sources
Beta strandi366 – 3727Combined sources
Beta strandi380 – 3856Combined sources
Helixi397 – 3993Combined sources
Beta strandi405 – 4128Combined sources
Beta strandi440 – 4478Combined sources
Turni452 – 4565Combined sources
Beta strandi459 – 4657Combined sources
Beta strandi479 – 4835Combined sources
Beta strandi489 – 4968Combined sources
Beta strandi505 – 5084Combined sources
Beta strandi512 – 5198Combined sources
Beta strandi521 – 5233Combined sources
Beta strandi525 – 5317Combined sources
Beta strandi533 – 54311Combined sources
Turni549 – 5524Combined sources
Beta strandi553 – 5564Combined sources
Beta strandi558 – 5658Combined sources
Beta strandi576 – 5816Combined sources
Beta strandi583 – 59210Combined sources
Beta strandi598 – 6069Combined sources
Helixi607 – 6115Combined sources
Beta strandi615 – 6217Combined sources
Helixi623 – 6264Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GYRX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L32-643[»]
ProteinModelPortaliQ53692.
SMRiQ53692. Positions 38-629.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 224138Plastocyanin-like 1Sequence analysisAdd
BLAST
Domaini494 – 621128Plastocyanin-like 2Sequence analysisAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

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 AAA86668.1 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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3GYRX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L32-643[»]
ProteinModelPortaliQ53692.
SMRiQ53692. Positions 38-629.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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...

Publicationsi

  1. "Nucleotide sequence, transcriptional analysis, and glucose regulation of the phenoxazinone synthase gene (phsA) from Streptomyces antibioticus."
    Hsieh C.-J., Jones G.H.
    J. Bacteriol. 177:5740-5747(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16.
    Strain: DSM 41481 / IMRU 3720.
  2. "Phenoxazinone synthetase from Streptomyces antibioticus: multiple activities of the enzyme."
    Golub E.E., Nishimura J.S.
    J. Bacteriol. 112:1353-1357(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
  3. "Phenoxazinone synthase from Streptomyces antibiotics: purification of the large and small enzyme forms."
    Choy H.A., Jones G.H.
    Arch. Biochem. Biophys. 211:55-65(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  4. "Phenoxazinone synthase: mechanism for the formation of the phenoxazinone chromophore of actinomycin."
    Barry C.E. III, Nayar P.G., Begley T.P.
    Biochemistry 28:6323-6333(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.
  5. "Crystallization and initial X-ray analysis of phenoxazinone synthase from Streptomyces antibioticus."
    Smith A.W., Camara-Artigas A., Olea C. Jr., Francisco W.A., Allen J.P.
    Acta Crystallogr. D 60:1453-1455(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, SUBUNIT.
  6. "Actinomycin production persists in a strain of Streptomyces antibioticus lacking phenoxazinone synthase."
    Jones G.H.
    Antimicrob. Agents Chemother. 44:1322-1327(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: REVIEW, FUNCTION, COFACTOR.
  8. "Structure of phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center."
    Smith A.W., Camara-Artigas A., Wang M., Allen J.P., Francisco W.A.
    Biochemistry 45:4378-4387(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 32-643 IN COMPLEX WITH COPPER IONS, SUBUNIT, COFACTOR.

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: March 16, 2016
This is version 81 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.