ID N0AW17_9BACI Unreviewed; 534 AA.
AC N0AW17;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=4-hydroxyphenylacetate 3-hydroxylase {ECO:0000313|EMBL:AGK55334.1};
GN ORFNames=B1NLA3E_17950 {ECO:0000313|EMBL:AGK55334.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK55334.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK55334.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK55334.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
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DR EMBL; CP005586; AGK55334.1; -; Genomic_DNA.
DR AlphaFoldDB; N0AW17; -.
DR STRING; 666686.B1NLA3E_17950; -.
DR KEGG; baci:B1NLA3E_17950; -.
DR eggNOG; COG2368; Bacteria.
DR HOGENOM; CLU_023920_2_1_9; -.
DR Proteomes; UP000013300; Chromosome.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000013300}.
FT DOMAIN 45..307
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 326..507
FT /note="HpaB/PvcC/4-BUDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03241"
FT BINDING 191..194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 488..491
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ SEQUENCE 534 AA; 60681 MW; C495D63B0947DAEB CRC64;
MKNIKINTLT GQPIALDRNI AFYIPSRAFV FKGVDCLMKT KKKSGFKESL NDGRSVWLNG
KKIKDLANHP EFTGTLKTIT SLWETLDSPD EQQKVGFISP RTNEYVHKAY LIPNNLKDLK
SRRESFALWS RKTFGVMSRL SDYSSSLITG YFIDRDYFNQ FDPGFSKKIT AYYEQARDER
RVITTAILDP QIDRSKPNDE HQDQDALLRV IQETEEGVIV RGAKMIATAA PYAHDVIVMP
HQKLSPGKSE YANMFIVPLN LPGLQIVCRE SFASQDQKKH PLSAQFDEMD AVLIFDDVLI
PWERVLIRGS AEGVFEAQQH QQLNGLAHHQ TVVRLLTKLQ FVAGVTTAIA QSIGADHFLH
VQEKLGELYT QIDSIEALLI ASEVQGSLND KKVYMPARVP LITARNLGTR YYPRAIEILK
QIGAGGFIQL PSTTVNDSNE LTPFFEKYYR GAKVDAMTKT ALFQVGWELV GSTLGARHDL
YERFYTGDPI RTFAFQYDTY DKEPLKQKLA LFWEELHGKE KLDEQNNPVP STTR
//
