ID A3JVK5_9RHOB Unreviewed; 373 AA.
AC A3JVK5;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Probable 4-hydroxyphenylpyruvate dioxygenase protein {ECO:0000313|EMBL:EBA02387.1};
GN ORFNames=RB2150_16477 {ECO:0000313|EMBL:EBA02387.1};
OS Rhodobacteraceae bacterium HTCC2150.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA02387.1, ECO:0000313|Proteomes:UP000004731};
RN [1] {ECO:0000313|EMBL:EBA02387.1, ECO:0000313|Proteomes:UP000004731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA02387.1,
RC ECO:0000313|Proteomes:UP000004731};
RX PubMed=20889754; DOI=10.1128/JB.01088-10;
RA Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT the Roseobacter clade.";
RL J. Bacteriol. 192:6315-6316(2010).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR009283-1};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR009283-1};
CC -!- SIMILARITY: Belongs to the 4HPPD family.
CC {ECO:0000256|ARBA:ARBA00005877}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EBA02387.1}.
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DR EMBL; AAXZ01000010; EBA02387.1; -; Genomic_DNA.
DR AlphaFoldDB; A3JVK5; -.
DR eggNOG; COG3185; Bacteria.
DR Proteomes; UP000004731; Unassembled WGS sequence.
DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR CDD; cd07250; HPPD_C_like; 1.
DR CDD; cd08342; HPPD_N_like; 1.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR InterPro; IPR005956; 4OHPhenylPyrv_dOase.
DR InterPro; IPR041735; 4OHPhenylPyrv_dOase_C.
DR InterPro; IPR041736; 4OHPhenylPyrv_dOase_N.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR037523; VOC.
DR NCBIfam; TIGR01263; 4HPPD; 1.
DR PANTHER; PTHR11959; 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE; 1.
DR PANTHER; PTHR11959:SF1; 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR Pfam; PF14696; Glyoxalase_5; 1.
DR PIRSF; PIRSF009283; HPP_dOase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR PROSITE; PS51819; VOC; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:EBA02387.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR009283-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR009283-1};
KW Oxidoreductase {ECO:0000313|EMBL:EBA02387.1};
KW Pyruvate {ECO:0000313|EMBL:EBA02387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004731};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 173..329
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 254
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 338
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ SEQUENCE 373 AA; 41402 MW; 344047F9456E4C4D CRC64;
MNQIAENFMG PFPHDAPTAK ISDLNPAGTD GFEFVEFAHE NPQELRNLFL QMGYSHTATH
KTKQIELWQQ GDITYVLNAE PGSMGMNYVA DHGPCAPSMA WRVVDAQHAF DHAVAKGAKP
YTGGGKVLDV PAIVGIGGSL LYFVETYGYN GNAYTTEYDW ITEPAPKGVG FFYLDHLTHN
VKRGNMDIWF SFYADIFNFK QIRFFDIAGK HTGLFSRALT SPCGRIRIPI NESADENSQI
EEYLRAYNGE GIQHIAVATN DIYGATDKIH ANGLEFMPPP PAAYYQMSGM RVLNHQEPID
QLSKHGILID GEGVVDGGIT RVLLQIFSKT VIGPIFFEFI QRKGDDGFGE GNFKALFESI
EQDQIDRGVL KAS
//