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Database: UniProt
Entry: F7QKC6_9BRAD
LinkDB: F7QKC6_9BRAD
Original site: F7QKC6_9BRAD 
ID   F7QKC6_9BRAD            Unreviewed;       491 AA.
AC   F7QKC6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=4-hydroxyphenylacetate 3-monooxygenase {ECO:0000313|EMBL:EGP08295.1};
DE            EC=1.14.14.9 {ECO:0000313|EMBL:EGP08295.1};
GN   ORFNames=CSIRO_2021 {ECO:0000313|EMBL:EGP08295.1};
OS   Bradyrhizobiaceae bacterium SG-6C.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae.
OX   NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP08295.1, ECO:0000313|Proteomes:UP000003148};
RN   [1] {ECO:0000313|EMBL:EGP08295.1, ECO:0000313|Proteomes:UP000003148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG-6C {ECO:0000313|EMBL:EGP08295.1,
RC   ECO:0000313|Proteomes:UP000003148};
RX   PubMed=21742875; DOI=10.1128/JB.05647-11;
RA   Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G.,
RA   Pandey G.;
RT   "Genome Sequence of the Newly Isolated Chemolithoautotrophic
RT   Bradyrhizobiaceae Strain SG-6C.";
RL   J. Bacteriol. 193:5057-5057(2011).
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:EGP08295.1}.
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DR   EMBL; AFOF01000023; EGP08295.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7QKC6; -.
DR   STRING; 709797.CSIRO_2021; -.
DR   eggNOG; COG2368; Bacteria.
DR   HOGENOM; CLU_023920_2_1_5; -.
DR   Proteomes; UP000003148; Chromosome.
DR   GO; GO:0052881; F:4-hydroxyphenylacetate 3-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.3140.10; 4-hydroxybutyryl-coa dehydratase, domain 1; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR004925; HpaB/PvcC/4-BUDH.
DR   InterPro; IPR024719; HpaB/PvcC/4-BUDH_C.
DR   InterPro; IPR024674; HpaB/PvcC/4-BUDH_N.
DR   PANTHER; PTHR36117; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR36117:SF3; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF03241; HpaB; 1.
DR   Pfam; PF11794; HpaB_N; 1.
DR   PIRSF; PIRSF000331; HpaA_HpaB; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|PIRSR:PIRSR000331-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:EGP08295.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EGP08295.1}.
FT   DOMAIN          6..269
FT                   /note="HpaB/PvcC/4-BUDH N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11794"
FT   DOMAIN          276..476
FT                   /note="HpaB/PvcC/4-BUDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03241"
FT   BINDING         151..154
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         188
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ   SEQUENCE   491 AA;  54300 MW;  504C51D12BACBD2B CRC64;
     MMRSAKDYLS SLNDGRTIYI NGSAVDDVTT HHAFRNVATS MAGLFDFASA PANQELMTFD
     NDGARANRIW QLPTSYAELV ERRKALEAWA SLHGGFMGRA PDHVASCISG LYMGLDVFKA
     YDPARAGALE SYYRYARDND LYLTYVIINP QADRSKGAAE QADPFLTAGV VDKDAEGITI
     RGAKMLATGG VVADEVFVTT IQPMRPGEER YAMSFAIPMN TKGLKMLSRK SYEDAAGAVF
     DNPLSSRFDE NDSILYFDDV KVPWDRVFIE GNVEMCQKQF HATPCHVYQN YQAMVRLSVK
     LKFLAGLAHR TAEMNGVTQF PQVREMLGQL AAETGMVDAL VAAMEAKGAH IGPYFIPHRH
     TLYAAQVLTQ QLYSHIVNTL RELAGGGMIM LPSSITDFAN PEIASLIEKT QQSPKANSHD
     RVKFYKLAWD AVGSEFGSRH QQYEMFYAGA TFVTKGHSYR TYDWAGSDAL VQRMLDSYDM
     SGGIVSPSKA A
//
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