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UniProtKB/Swiss-Prot entry P30967


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PH4H_CHRVO
Primary accession number P30967
Secondary accession numbers Q9R634 Q9XC88
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on October 24, 2003 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 87)
Name and origin of the protein
Protein name Phenylalanine-4-hydroxylase
Synonyms PAH
EC 1.14.16.1
Phe-4-monooxygenase
Gene name
Name: phhA
OrderedLocusNames: CV_3180
From
Chromobacterium violaceum [TaxID: 536] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Chromobacterium.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
STRAIN=ATCC 12540 / NCTC 9695;
PubMed=1655752 [NCBI, ExPASy, EBI, Israel, Japan]
Onishi A., Liotta L.J., Benkovic S.J.;
"Cloning and expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroxylases.";
J. Biol. Chem. 266:18454-18459(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 12540 / NCTC 9695;
Volner A., Nersissian A.M., Abu-Omar M.M.;
"Expression, isolation, and metal-dependent catalysis of phenylalanine hydroxylase from Chromobacterium violaceum.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131;
DOI=10.1073/pnas.1832124100; PubMed=14500782 [NCBI, ExPASy, EBI, Israel, Japan]
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability.";
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
[4]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
DOI=10.1016/S0022-2836(02)00496-5; PubMed=12096915 [NCBI, ExPASy, EBI, Israel, Japan]
Erlandsen H., Kim J.Y., Patch M.G., Han A., Volner A., Abu-Omar M.M., Stevens R.C.;
"Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates.";
J. Mol. Biol. 320:645-661(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M55915; AAA23115.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146711; AAD37774.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE016825; AAQ60846.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A40996; A40996.
RefSeq NP_902850.1; -.
3D structure databases
PDB
1LTU; X-ray; 1.74 A; A=1-297.[ExPASy / RCSB / EBI]
1LTV; X-ray; 2.00 A; A=1-297.[ExPASy / RCSB / EBI]
1LTZ; X-ray; 1.40 A; A=1-297.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1LTU; -.
1LTV; -.
1LTZ; -.
ModBase P30967.
Enzyme and pathway databases
BioCyc CVIO243365:CV_3180-MON; -.
MetaCyc:MON-12067; -.
Family and domain databases
InterPro IPR001273; Aaa_hydroxylase.
IPR005960; Phe-4-hydroxylase_mono.
Graphical view of domain structure.
Gene3D G3DSA:1.10.800.10; Aaa_hydroxylase; 1.
PANTHER PTHR11473; Aaa_hydroxylase; 1.
Pfam PF00351; Biopterin_H; 2.
Pfam graphical view of domain structure.
PRINTS PR00372; FYWHYDRXLASE.
ProDom PD002559; Aaa_hydroxylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01267; Phe4hydrox_mono; 1.
PROSITE PS00367; BIOPTERIN_HYDROXYL; 1.
BLOCKS P30967.
Genome annotation databases
GeneID 2548525; -.
GenomeReviews AE016825_GR; CV_3180.
KEGG cvi:CV_3180; -.
NMPDR fig|243365.1.peg.3180; -.
Phylogenomic databases
HOGENOM P30967; -.
Genome annotation databases
CMR P30967; CV_3180.
Other
ProtoNet P30967.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phenylalanine catabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   297  297     Phenylalanine-4-hydroxylase. PRO_0000205553
METAL   138   138        Iron. 
METAL   143   143        Iron. 
METAL   184   184        Iron. 
CONFLICT   64    64        M -> L (in Ref. 1 and 2). 
CONFLICT   85    85        Q -> E (in Ref. 1 and 2). 
CONFLICT   276   276        V -> I (in Ref. 1 and 2). 
CONFLICT   288   288        R -> H (in Ref. 1 and 2). 
HELIX   12    16  5      
TURN   17    19  3      
TURN   24    26  3      
HELIX   33    35  3      
HELIX   38    54  17      
TURN   56    58  3      
HELIX   61    70  10      
STRAND   74    76  3      
HELIX   80    91  12      
STRAND   94   100  7      
HELIX   104   112  9      
STRAND   115   119  5      
STRAND   128   130  3      
HELIX   136   142  7      
HELIX   144   148  5      
HELIX   150   165  16      
HELIX   171   181  11      
TURN   182   185  4      
STRAND   187   190  4      
STRAND   193   196  4      
HELIX   199   202  4      
HELIX   205   210  6      
STRAND   215   221  7      
HELIX   224   228  5      
STRAND   234   236  3      
STRAND   239   245  7      
HELIX   247   252  6      
HELIX   259   265  7      
Sequence information
Length: 297 AA [This is the length of the unprocessed precursor] Molecular weight: 33616 Da [This is the MW of the unprocessed precursor] CRC64: 6D29A04203E906FD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNDRADFVVP DITTRKNVGL SHDANDFTLP QPLDRYSAED HATWATLYQR QCKLLPGRAC 

        70         80         90        100        110        120 
DEFMEGLERL EVDADRVPDF NKLNQKLMAA TGWKIVAVPG LIPDDVFFEH LANRRFPVTW 

       130        140        150        160        170        180 
WLREPHQLDY LQEPDVFHDL FGHVPLLINP VFADYLEAYG KGGVKAKALG ALPMLARLYW 

       190        200        210        220        230        240 
YTVEFGLINT PAGMRIYGAG ILSSKSESIY CLDSASPNRV GFDLMRIMNT RYRIDTFQKT 

       250        260        270        280        290 
YFVIDSFKQL FDATAPDFAP LYLQLADAQP WGAGDVAPDD LVLNAGDRQG WADTEDV 

P30967 in FASTA format

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