ID A0A102D540_9SPHN Unreviewed; 484 AA.
AC A0A102D540;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aromatic ring hydroxylase {ECO:0000313|EMBL:KUR75164.1};
GN ORFNames=AQZ50_16200 {ECO:0000313|EMBL:KUR75164.1};
OS Novosphingobium sp. Fuku2-ISO-50.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR75164.1, ECO:0000313|Proteomes:UP000056630};
RN [1] {ECO:0000313|EMBL:KUR75164.1, ECO:0000313|Proteomes:UP000056630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR75164.1,
RC ECO:0000313|Proteomes:UP000056630};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM 27930), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUR75164.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LLZR01000023; KUR75164.1; -; Genomic_DNA.
DR RefSeq; WP_067747803.1; NZ_KQ954299.1.
DR AlphaFoldDB; A0A102D540; -.
DR STRING; 1739114.AQZ50_16200; -.
DR OrthoDB; 7233724at2; -.
DR Proteomes; UP000056630; Unassembled WGS sequence.
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:UP000056630}.
FT DOMAIN 6..269
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 290..473
FT /note="HpaB/PvcC/4-BUDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03241"
FT BINDING 146..148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 189
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ SEQUENCE 484 AA; 54238 MW; 6CC8466A7BBB8ABD CRC64;
MAVRNGQQFL AGLKDDRVVY LGDRKVDTLT EPRFQGSLQG MAEYFDYQIE NADDCLVADP
EKPGEMMSAS LIVPRNKEDL AIRHKALDRF ARYSYGMLGR TPDYVNVVLS GHVARRDIWE
KGDPVYHDRL TKFHREVIDG DLSLTHAIAH ANIDKSTGDL AGMNADLTVH KVGETQNGII
VRGGKMLATL GPFTDEFYVY PSAPIPTRAE RHALCFSVPS NTKGLIMFCR DHYGVDESRA
DAPFSSRFDE QDVFVVFDDV EVPYERLFID GNLDVYNNVT RGVSPGNTLQ QTAIRAKVKL
EFAYDLCTLM ARITGSEQRQ DVAVMLGEIH TYMIMTKAAI IAAEERAHVW GTSGAFFPHR
DLAALRSIMP EWMSRVNQII RALGSHNMLA TPSLDLFQDP DVGDMLRKYL PGANGFTAEQ
RAAVFRTARD FAISALAGRN ELYEMFYLGS LNRARAGDHM VAQRNGWKGE VMEFLTKNGA
FLKK
//
