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Database: UniProt
Entry: A0A0U4NGG8_9BACL
LinkDB: A0A0U4NGG8_9BACL
Original site: A0A0U4NGG8_9BACL 
ID   A0A0U4NGG8_9BACL        Unreviewed;       488 AA.
AC   A0A0U4NGG8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=4-hydroxyphenylacetate 3-monooxygenase/anthranilate 3-monooxygenase (FAD)/4-hydroxyphenylacetate 3-monooxygenase {ECO:0000313|EMBL:PYE61343.1};
DE   SubName: Full=Anthranilate 3-monooxygenase oxygenase component {ECO:0000313|EMBL:BAU27828.1};
DE            EC=1.14.14.8 {ECO:0000313|EMBL:BAU27828.1};
GN   Name=hpaH {ECO:0000313|EMBL:BAU27828.1};
GN   ORFNames=CB4_02002 {ECO:0000313|EMBL:BAU27828.1}, DFP93_10942
GN   {ECO:0000313|EMBL:PYE61343.1};
OS   Aneurinibacillus soli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=1500254 {ECO:0000313|EMBL:BAU27828.1, ECO:0000313|Proteomes:UP000217696};
RN   [1] {ECO:0000313|EMBL:BAU27828.1, ECO:0000313|Proteomes:UP000217696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB4 {ECO:0000313|EMBL:BAU27828.1,
RC   ECO:0000313|Proteomes:UP000217696};
RA   Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT   "Genome sequence of Aneurinibacillus soli.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PYE61343.1, ECO:0000313|Proteomes:UP000247363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8566 {ECO:0000313|EMBL:PYE61343.1,
RC   ECO:0000313|Proteomes:UP000247363};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AP017312; BAU27828.1; -; Genomic_DNA.
DR   EMBL; QJSZ01000009; PYE61343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U4NGG8; -.
DR   KEGG; asoc:CB4_02002; -.
DR   OrthoDB; 9785230at2; -.
DR   Proteomes; UP000217696; Chromosome.
DR   Proteomes; UP000247363; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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:BAU27828.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:BAU27828.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217696}.
FT   DOMAIN          5..271
FT                   /note="HpaB/PvcC/4-BUDH N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11794"
FT   DOMAIN          291..477
FT                   /note="HpaB/PvcC/4-BUDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03241"
FT   BINDING         148..150
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         154..157
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         191
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         452..455
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ   SEQUENCE   488 AA;  55017 MW;  B4EBE809E7ABE60E CRC64;
     MAVRTGQQFL EGLKNDGREI WLDGELIQDV TTHPAFKGAA EHIAKLFDLQ HKYPEIMTAT
     CPETGEKFGI THLIPRSKED IKRIRKAMKV WAEASVGLMG RSPDYMNTTF ACFAGHADVW
     ARRGNEQGAR NMIAYQKYVR DNDLIMTHSI INPQVDRSVS EAEQGGGEVS LHKVGETEDS
     IIVRGARMLA TLAPFADELT VYPGSDIRLQ DKKYAICFAV PMNTPGLKFI CRDSYSKERN
     NFDYPLSSRF DEMDAVVIFD DVHVPKDRVF MDGDTVGYSE VIGDGYWRNY IIFQAMNRAL
     TKLEFAFGLG HMIADTTGVN AFDHVQEKLG EIWNMMEMTR AGVVAAEEGA FEVDGKGIWA
     PDDKPLIALR GLMPKWIPRA TELLKVIGGG GYMLTPSLKD MNGPLANDIT KYYQARNADA
     EQRIRLFRLG WDFIGSELAG RGDLYERFYL SDAYRMTALN YKVAEKEHAE MLVKQFLNEP
     VNELQATK
//
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