ID A0A0S8IMW5_9BACT Unreviewed; 508 AA.
AC A0A0S8IMW5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Aromatic ring hydroxylase {ECO:0000313|EMBL:KPK97661.1};
GN ORFNames=AMJ95_08025 {ECO:0000313|EMBL:KPK97661.1};
OS Omnitrophica WOR_2 bacterium SM23_72.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1703777 {ECO:0000313|EMBL:KPK97661.1, ECO:0000313|Proteomes:UP000051899};
RN [1] {ECO:0000313|EMBL:KPK97661.1, ECO:0000313|Proteomes:UP000051899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_72 {ECO:0000313|EMBL:KPK97661.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK97661.1}.
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DR EMBL; LJUU01000030; KPK97661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8IMW5; -.
DR PATRIC; fig|1703777.3.peg.1381; -.
DR Proteomes; UP000051899; 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}.
FT DOMAIN 7..268
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 284..477
FT /note="HpaB/PvcC/4-BUDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03241"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ SEQUENCE 508 AA; 57647 MW; 86F18E4EBC3D4265 CRC64;
MGVKSFDEYY GRLKKLKRNM YIGGEKVDRT DERLAGQLRV IKETYDRAND PDWEDLCTAT
SHLTGEKINR FTHIHQSVDD LLDKQLMTRL LCHRVGGCIM RCMGIDCMNA LSAVTYEMDK
ILGTDTNENF LKYLRYWQDN DICANCAQTD TKGDRIKRPH EQADPDLYLR IIESRPDGIV
VRGAKIDNTT APVSDEIIAI PTRFMTDKDH DYAVAFAVPA DWDGVKMLVR PAYHHRRNYL
KAPIAEVGDA ESFTIFDDVF VPRERVFLDG KGDSRQTPFA GFLALLFAHY HRHSYTGCKP
AVSEVLASAA ALVSEYNNIE REDHVRDKLS HLIGTAELVF AAGQMSAYRG ERSASGTYIP
DEILTNAGRR LAGEEIYNEY RIVADLAGGL CATMPFEEEF SSKETGELAS KYLMRNPKIS
SENQHRCFRG IENMIVSETA AVMQVAGLHG GGSPQMETIT MMARYDLESL KSIAKYLFGI
EKELPKYERP TVTPRKMLER FRRLVNRQ
//
