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Protein

3-phenylpropionate/cinnamic acid dioxygenase subunit alpha

Gene

hcaE

Organism
Shigella boydii serotype 4 (strain Sb227)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively.UniRule annotation

Catalytic activityi

3-phenylpropanoate + NADH + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+.UniRule annotation
(2E)-3-phenylprop-2-enoate + NADH + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NAD+.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Fe cationUniRule annotationNote: Binds 1 Fe cation.UniRule annotation
  • [2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster per subunit.UniRule annotation

Pathwayi: 3-phenylpropanoate degradation

This protein is involved in the pathway 3-phenylpropanoate degradation, which is part of Aromatic compound metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway 3-phenylpropanoate degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi85Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi87Iron-sulfur (2Fe-2S); via pros nitrogenUniRule annotation1
Metal bindingi105Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi108Iron-sulfur (2Fe-2S); via pros nitrogenUniRule annotation1
Metal bindingi213IronUniRule annotation1
Metal bindingi218IronUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processAromatic hydrocarbons catabolism
Ligand2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

UniPathwayiUPA00714

Names & Taxonomyi

Protein namesi
Recommended name:
3-phenylpropionate/cinnamic acid dioxygenase subunit alphaUniRule annotation (EC:1.14.12.19UniRule annotation)
Gene namesi
Name:hcaEUniRule annotation
Ordered Locus Names:SBO_2562
OrganismiShigella boydii serotype 4 (strain Sb227)
Taxonomic identifieri300268 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000007067 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003337061 – 4533-phenylpropionate/cinnamic acid dioxygenase subunit alphaAdd BLAST453

Interactioni

Subunit structurei

This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (HcaE and HcaF), a ferredoxin (HcaC) and a ferredoxin reductase (HcaD).UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ31XV2
SMRiQ31XV2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 142RieskeUniRule annotationAdd BLAST99

Sequence similaritiesi

Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000105925
KOiK05708
OMAiGEYCEDF

Family and domain databases

Gene3Di2.102.10.10, 1 hit
HAMAPiMF_01648 HcaE, 1 hit
InterProiView protein in InterPro
IPR020875 HcaE
IPR017941 Rieske_2Fe-2S
IPR036922 Rieske_2Fe-2S_sf
IPR015881 Ring-hydroxy_dOase_2Fe2S_BS
IPR015879 Ring_hydroxy_dOase_asu_C_dom
IPR001663 Rng_hydr_dOase-A
PfamiView protein in Pfam
PF00355 Rieske, 1 hit
PF00848 Ring_hydroxyl_A, 1 hit
PRINTSiPR00090 RNGDIOXGNASE
SUPFAMiSSF50022 SSF50022, 1 hit
PROSITEiView protein in PROSITE
PS51296 RIESKE, 1 hit
PS00570 RING_HYDROXYL_ALPHA, 1 hit

Sequencei

Sequence statusi: Complete.

Q31XV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTPSDLNIY QLIDTQNGRV TPRIYTDPDI YQLELERIFG RCWLFLAHES
60 70 80 90 100
QIPKPGDFFN TYMGEDAVVV VRQKDGSIKA FLNQCRHRAM RVSYADCGNT
110 120 130 140 150
RAFTCPYHGW SYGINGELID VPLEPRAYPQ GLCKSHWGLN EVPCVESYKG
160 170 180 190 200
LIFGNWDTSA PGLRDYLGDI AWYLDGMLDR REGGTEIVGG VQKWVINCNW
210 220 230 240 250
KSPAEQFASD QYHALFSHAS AVQVLGAKDD GSDKRLGDGQ TARPVWETAK
260 270 280 290 300
DALQFGQDGH GSGFFFTEKP DANVWVDGAV SSYYRETYAE AEQRLGEVRA
310 320 330 340 350
LRLAGHNNIF PTLSWLNGTA TLRVWHPRGP DQVEVWAFCI TDKAASDEVK
360 370 380 390 400
AAFENSATRA FGPAGFLEQD DSENWCEIQK LLKGHRARNS KLCLEMGLGQ
410 420 430 440 450
EKRRDDGIPG ITNYIFSETA ARGMYQRWAD LLSSESWQEV LDKTAAYQQE

VMK
Length:453
Mass (Da):51,049
Last modified:December 6, 2005 - v1
Checksum:i43535BF0F57643F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000036 Genomic DNA Translation: ABB67106.1

Genome annotation databases

EnsemblBacteriaiABB67106; ABB67106; SBO_2562
KEGGisbo:SBO_2562

Similar proteinsi

Entry informationi

Entry nameiHCAE_SHIBS
AccessioniPrimary (citable) accession number: Q31XV2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 6, 2005
Last modified: March 28, 2018
This is version 80 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
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Main funding by: National Institutes of Health