PH4H_CHRVO
ID PH4H_CHRVO Reviewed; 297 AA.
AC P30967; Q9R634; Q9XC88;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Phenylalanine-4-hydroxylase;
DE Short=PAH;
DE EC=1.14.16.1;
DE AltName: Full=Phe-4-monooxygenase;
GN Name=phhA; OrderedLocusNames=CV_3180;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RC STRAIN=ATCC 12540 / LMG 3962 / NCTC 9695;
RX PubMed=1655752; DOI=10.1016/s0021-9258(18)55083-3;
RA Onishi A., Liotta L.J., Benkovic S.J.;
RT "Cloning and expression of Chromobacterium violaceum phenylalanine
RT hydroxylase in Escherichia coli and comparison of amino acid sequence with
RT mammalian aromatic amino acid hydroxylases.";
RL J. Biol. Chem. 266:18454-18459(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12540 / LMG 3962 / NCTC 9695;
RA Volner A., Nersissian A.M., Abu-Omar M.M.;
RT "Expression, isolation, and metal-dependent catalysis of phenylalanine
RT hydroxylase from Chromobacterium violaceum.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX PubMed=12096915; DOI=10.1016/s0022-2836(02)00496-5;
RA Erlandsen H., Kim J.Y., Patch M.G., Han A., Volner A., Abu-Omar M.M.,
RA Stevens R.C.;
RT "Structural comparison of bacterial and human iron-dependent phenylalanine
RT hydroxylases: similar fold, different stability and reaction rates.";
RL J. Mol. Biol. 320:645-661(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine +
CC O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-
CC tyrosine; Xref=Rhea:RHEA:20273, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642,
CC ChEBI:CHEBI:58095, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560;
CC EC=1.14.16.1;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 1/6.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC hydroxylase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23115.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M55915; AAA23115.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF146711; AAD37774.1; -; Genomic_DNA.
DR EMBL; AE016825; AAQ60846.1; -; Genomic_DNA.
DR PIR; A40996; A40996.
DR PDB; 1LTU; X-ray; 1.74 A; A=1-297.
DR PDB; 1LTV; X-ray; 2.00 A; A=1-297.
DR PDB; 1LTZ; X-ray; 1.40 A; A=1-297.
DR PDB; 3TCY; X-ray; 1.55 A; A=1-297.
DR PDB; 3TK2; X-ray; 1.35 A; A=1-297.
DR PDB; 3TK4; X-ray; 1.50 A; A=1-297.
DR PDB; 4ESM; X-ray; 1.35 A; A=1-297.
DR PDB; 4ETL; X-ray; 1.49 A; A=1-297.
DR PDB; 4JPX; X-ray; 1.55 A; A=1-297.
DR PDB; 4JPY; X-ray; 2.13 A; A=1-297.
DR PDB; 4Q3W; X-ray; 1.40 A; A=1-297.
DR PDB; 4Q3X; X-ray; 1.35 A; A=1-297.
DR PDB; 4Q3Y; X-ray; 1.40 A; A=1-297.
DR PDB; 4Q3Z; X-ray; 1.35 A; A=1-297.
DR PDBsum; 1LTU; -.
DR PDBsum; 1LTV; -.
DR PDBsum; 1LTZ; -.
DR PDBsum; 3TCY; -.
DR PDBsum; 3TK2; -.
DR PDBsum; 3TK4; -.
DR PDBsum; 4ESM; -.
DR PDBsum; 4ETL; -.
DR PDBsum; 4JPX; -.
DR PDBsum; 4JPY; -.
DR PDBsum; 4Q3W; -.
DR PDBsum; 4Q3X; -.
DR PDBsum; 4Q3Y; -.
DR PDBsum; 4Q3Z; -.
DR AlphaFoldDB; P30967; -.
DR SMR; P30967; -.
DR STRING; 243365.CV_3180; -.
DR EnsemblBacteria; AAQ60846; AAQ60846; CV_3180.
DR KEGG; cvi:CV_3180; -.
DR eggNOG; COG3186; Bacteria.
DR HOGENOM; CLU_023198_1_0_4; -.
DR OMA; KQFPVAT; -.
DR BioCyc; MetaCyc:MON-12067; -.
DR BRENDA; 1.14.16.1; 1370.
DR UniPathway; UPA00139; UER00337.
DR EvolutionaryTrace; P30967; -.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IDA:CACAO.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03348; pro_PheOH; 1.
DR Gene3D; 1.10.800.10; -; 1.
DR InterPro; IPR001273; ArAA_hydroxylase.
DR InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR InterPro; IPR036951; ArAA_hydroxylase_sf.
DR InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
DR InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR InterPro; IPR005960; Phe-4-hydroxylase_mono.
DR PANTHER; PTHR11473; PTHR11473; 1.
DR Pfam; PF00351; Biopterin_H; 1.
DR PRINTS; PR00372; FYWHYDRXLASE.
DR SUPFAM; SSF56534; SSF56534; 1.
DR TIGRFAMs; TIGR01267; Phe4hydrox_mono; 1.
DR PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Iron; Metal-binding;
KW Monooxygenase; Oxidoreductase; Phenylalanine catabolism;
KW Reference proteome.
FT CHAIN 1..297
FT /note="Phenylalanine-4-hydroxylase"
FT /id="PRO_0000205553"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 143
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT CONFLICT 64
FT /note="M -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="Q -> E (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="V -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="R -> H (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:3TK2"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:3TK2"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:3TK2"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:3TK2"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:3TK2"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:3TK2"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3TK2"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1LTZ"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:3TK2"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:3TK2"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1LTZ"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1LTZ"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:3TK2"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:3TK2"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3TK2"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:3TK2"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:3TK2"
SQ SEQUENCE 297 AA; 33616 MW; 6D29A04203E906FD CRC64;
MNDRADFVVP DITTRKNVGL SHDANDFTLP QPLDRYSAED HATWATLYQR QCKLLPGRAC
DEFMEGLERL EVDADRVPDF NKLNQKLMAA TGWKIVAVPG LIPDDVFFEH LANRRFPVTW
WLREPHQLDY LQEPDVFHDL FGHVPLLINP VFADYLEAYG KGGVKAKALG ALPMLARLYW
YTVEFGLINT PAGMRIYGAG ILSSKSESIY CLDSASPNRV GFDLMRIMNT RYRIDTFQKT
YFVIDSFKQL FDATAPDFAP LYLQLADAQP WGAGDVAPDD LVLNAGDRQG WADTEDV
