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Protein

4-hydroxymandelate synthase

Gene
N/A
Organism
Amycolatopsis orientalis (Nocardia orientalis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required to synthesize hydroxyphenylglycine, a recurring skeletal component of nonproteinogenic macrocyclic peptide antibiotics such as vancomycin. Catalyzes the conversion of p-hydroxyphenylpyruvate to p-hydroxymandelate. The decarboxylation and hydroxylation activities of HmaS show novel and distinct regioselectivity, compared to all other known p-hydroxyphenylpyruvate dioxygenases, by hydroxylating the benzylic position of the substrate instead of the phenyl ring.1 Publication

Catalytic activityi

4-hydroxyphenylpyruvate + O2 = (S)-4-hydroxymandelate + CO2.1 Publication

Cofactori

Fe cation1 PublicationNote: Binds 1 Fe cation per subunit.1 Publication

Pathwayi: vancomycin biosynthesis

This protein is involved in the pathway vancomycin biosynthesis, which is part of Antibiotic biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway vancomycin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi161 – 1611Iron
Binding sitei201 – 2011Substrate1 Publication
Binding sitei214 – 2141Substrate1 Publication
Metal bindingi241 – 2411Iron
Binding sitei241 – 2411Substrate1 Publication
Binding sitei305 – 3051Substrate1 Publication
Metal bindingi320 – 3201Iron

GO - Molecular functioni

  • 4-hydroxymandelate synthase activity Source: UniProtKB
  • 4-hydroxyphenylpyruvate dioxygenase activity Source: InterPro
  • iron ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00162.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxymandelate synthase (EC:1.13.11.46)
Short name:
HMS
Short name:
HmaS
Alternative name(s):
4-hydroxyphenylpyruvate dioxygenase II
OrganismiAmycolatopsis orientalis (Nocardia orientalis)
Taxonomic identifieri31958 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeAmycolatopsis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3573574-hydroxymandelate synthasePRO_0000418534Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
357
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Helixi16 – 2712Combined sources
Beta strandi30 – 378Combined sources
Beta strandi40 – 478Combined sources
Beta strandi50 – 5910Combined sources
Helixi64 – 718Combined sources
Beta strandi72 – 8312Combined sources
Helixi85 – 9410Combined sources
Beta strandi99 – 1046Combined sources
Beta strandi113 – 1175Combined sources
Beta strandi123 – 1286Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi158 – 1658Combined sources
Helixi171 – 18212Combined sources
Beta strandi185 – 19410Combined sources
Beta strandi197 – 2059Combined sources
Beta strandi212 – 2187Combined sources
Helixi226 – 2349Combined sources
Beta strandi236 – 24510Combined sources
Helixi249 – 25810Combined sources
Helixi268 – 2725Combined sources
Turni273 – 2775Combined sources
Beta strandi281 – 2833Combined sources
Helixi285 – 2917Combined sources
Beta strandi294 – 2985Combined sources
Beta strandi301 – 3088Combined sources
Beta strandi318 – 3269Combined sources
Helixi332 – 34716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R5VX-ray2.30A/B1-357[»]
ProteinModelPortaliO52791.
SMRiO52791. Positions 2-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO52791.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni161 – 1611Substrate binding

Sequence similaritiesi

Belongs to the 4HPPD family.Curated

Phylogenomic databases

KOiK16421.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR005956. 4OHPhenylPyrv_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view]
PANTHERiPTHR11959. PTHR11959. 1 hit.
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
PIRSFiPIRSF009283. HPP_dOase. 1 hit.
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR01263. 4HPPD. 1 hit.

Sequencei

Sequence statusi: Complete.

O52791-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNFEIDYVE MYVENLEVAA FSWVDKYAFA VAGTSRSADH RSIALRQGQV
60 70 80 90 100
TLVLTEPTSD RHPAAAYLQT HGDGVADIAM ATSDVAAAYE AAVRAGAEAV
110 120 130 140 150
RAPGQHSEAA VTTATIGGFG DVVHTLIQRD GTSAELPPGF TGSMDVTNHG
160 170 180 190 200
KGDVDLLGID HFAICLNAGD LGPTVEYYER ALGFRQIFDE HIVVGAQAMN
210 220 230 240 250
STVVQSASGA VTLTLIEPDR NADPGQIDEF LKDHQGAGVQ HIAFNSNDAV
260 270 280 290 300
RAVKALSERG VEFLKTPGAY YDLLGERITL QTHSLDDLRA TNVLADEDHG
310 320 330 340 350
GQLFQIFTAS THPRHTIFFE VIERQGAGTF GSSNIKALYE AVELERTGQS

EFGAARR
Length:357
Mass (Da):38,339
Last modified:June 1, 1998 - v1
Checksum:iF146FCE537CEF2CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223998 Genomic DNA. Translation: CAA11761.1.
PIRiT17470.

Genome annotation databases

KEGGiag:CAA11761.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223998 Genomic DNA. Translation: CAA11761.1.
PIRiT17470.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R5VX-ray2.30A/B1-357[»]
ProteinModelPortaliO52791.
SMRiO52791. Positions 2-348.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA11761.

Phylogenomic databases

KOiK16421.

Enzyme and pathway databases

UniPathwayiUPA00162.

Miscellaneous databases

EvolutionaryTraceiO52791.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR005956. 4OHPhenylPyrv_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view]
PANTHERiPTHR11959. PTHR11959. 1 hit.
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
PIRSFiPIRSF009283. HPP_dOase. 1 hit.
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR01263. 4HPPD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHMAS_AMYOR
AccessioniPrimary (citable) accession number: O52791
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.