ID F4CM04_PSEUX Unreviewed; 493 AA.
AC F4CM04;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=4-hydroxyphenylacetate 3-monooxygenase, oxygenase subunit {ECO:0000313|EMBL:AEA22491.1};
DE EC=5.3.3.3 {ECO:0000313|EMBL:AEA22491.1};
GN OrderedLocusNames=Psed_0216 {ECO:0000313|EMBL:AEA22491.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA22491.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA22491.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
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DR EMBL; CP002593; AEA22491.1; -; Genomic_DNA.
DR RefSeq; WP_013672432.1; NC_015312.1.
DR AlphaFoldDB; F4CM04; -.
DR SMR; F4CM04; -.
DR STRING; 675635.Psed_0216; -.
DR KEGG; pdx:Psed_0216; -.
DR eggNOG; COG2368; Bacteria.
DR HOGENOM; CLU_023920_2_1_11; -.
DR OrthoDB; 9785230at2; -.
DR Proteomes; UP000007809; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0050393; F:vinylacetyl-CoA delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0010124; P:phenylacetate catabolic process; 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 InterPro; IPR012687; HpaB_Deino-type.
DR NCBIfam; TIGR02309; HpaB-1; 1.
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 Isomerase {ECO:0000313|EMBL:AEA22491.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT DOMAIN 5..271
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 278..478
FT /note="HpaB/PvcC/4-BUDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03241"
FT BINDING 147..149
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 153..156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 453..456
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ SEQUENCE 493 AA; 54219 MW; 7A65441380FF99B1 CRC64;
MSVRTGAQYL ERLQKTPREV WLRGERVDDV TAHPAFARPT ARIAALYDMQ HDPAHRDVLT
RPGPNGPVGT AFVAPASYAD LVARREAYRL WSEATLGLMG RSPDFLNTTL LAFAEEPGVF
ARLGSRYADN VVRYYEYVRD NDLFLTHALI TPQTDRSKGS TAQADPFLHM GVVAETADGL
VVRGARMLAT LAPMADELII YNLPGLRPGD EKHAAVFAVP IETPGLRLIS REPFDDGTRN
RFDHPLSSHF EEADCLVVFD DVLVPWDRVF LHGDVALANA MYVETNLRQH TAHQTGVRGL
VKMQFVTGVA MKLAQTVGID GFLHVQQKLG ELIAATETCR ALLRAAEIDH ETSASGRSVR
PGFLPLQTLR MHLSSSYPRA AEVLQTLGAG GLLMMPSAAD FDSPISGDIA RYFQGAAGLD
ATDRVRLYKL AWDLCGDGFG QRAVQYERYY AGDPVRLYSM NYLAYDKTDA FALVDRALAL
AGDPAQAVAE VRP
//