ID A0A2A4SC48_9CHLR Unreviewed; 488 AA.
AC A0A2A4SC48;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=4-hydroxyphenylacetate 3-monooxygenase {ECO:0000313|EMBL:PCI18943.1};
GN ORFNames=COB68_06310 {ECO:0000313|EMBL:PCI18943.1};
OS SAR202 cluster bacterium.
OC Bacteria; Chloroflexota; SAR202 cluster.
OX NCBI_TaxID=2030829 {ECO:0000313|EMBL:PCI18943.1, ECO:0000313|Proteomes:UP000217661};
RN [1] {ECO:0000313|Proteomes:UP000217661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) 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:PCI18943.1}.
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DR EMBL; NVSQ01000016; PCI18943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4SC48; -.
DR Proteomes; UP000217661; 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|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000331-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:PCI18943.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 4..271
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 278..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 488 AA; 54080 MW; 4257A063E1EC98C5 CRC64;
MTRTGADYIK NVQDGRSIYL DGQLIENAAE HPAFRNALAT VARLYDFQAA SENEELMTFP
SPTSGGRVNR CWQLPRSHAE LVQRREAITA WAELTFGFMG RSPDHVASSL SGMAMGIDVF
QRHGEDRAKA LMDYFTYVRD NDLFVTYVIA NPRADHSKDV SQQEDETLVA AICDEDSQGV
TINGAKMLGT SAVIADELLV TTGAPLKPGE EMYAFSVAMP MATKGLKILP RKSYEASAVS
QFDNPLSSHL DENDAIILFD NVKVPWDRVF VHKDTEICRA QFTDTPAHMY QNYQAQVRMM
VKLRFLLGLA RKIAETNGIL SIPEVAGTLG YLAANTAMME GMVKGMEAGG VSYGPYFVPD
RGLLYATQVL SQQFYPQMVH HIRDLGGASM IMMPPSVADF GNPETASFIH RTQRSPVAEP
KDKVKLFKLA WDAVGSEFGS RQAQYEMFYA GGPFVTRGRS FQNYDWSTVT DMVDGLLESY
DLPESPIG
//