ID A0A1F8P4W8_9CHLR Unreviewed; 481 AA.
AC A0A1F8P4W8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=4-hydroxybutyryl-CoA dehydratase {ECO:0000313|EMBL:OGO18142.1};
GN ORFNames=A2Z14_13520 {ECO:0000313|EMBL:OGO18142.1};
OS Chloroflexi bacterium RBG_16_48_8.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797641 {ECO:0000313|EMBL:OGO18142.1, ECO:0000313|Proteomes:UP000177106};
RN [1] {ECO:0000313|EMBL:OGO18142.1, ECO:0000313|Proteomes:UP000177106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO18142.1}.
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DR EMBL; MGNI01000110; OGO18142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8P4W8; -.
DR STRING; 1797641.A2Z14_13520; -.
DR Proteomes; UP000177106; 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 3..272
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 279..478
FT /note="HpaB/PvcC/4-BUDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03241"
FT BINDING 189
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ SEQUENCE 481 AA; 53331 MW; 0480D6B7401260CB CRC64;
MKTSEEYVNS LRNLKRDVYL FGEKLEDPLD HPIIKPSTNA IAMTYELAHD SQFRNLATVP
SSLTGIPINR FTHLHQSAAE LVEKIKLQRV LGQKTAVCFQ RCVGWDAMNA LDSVTYELDE
AYGTEYHKRF RSFLGTVQEK DLVCDGAMTD VKGDRSLSPS QQADPDLYLH IVDERKDGMV
VRGAKVHQTG IVNSHEIIVM PTASIREEDA DYAISFAVPT DTPGITVILG RQSCDLRLME
GGVIDPGNIR FGGHEGLVIF EDVFVPWERV FMCREYAFAG MLVERFAAYH RQSYGGCKVG
LGDVAIGAAA LIAEYNGTDR ASHIRDKIVE MVHLNETLYS CGLACSSEGK ATGTGTYLVD
IILANVTKHN TTRFPYEILR LLEDIAGGLL VTLPSEKDFR HPEIGPKIDK YLKGKAGVPT
ENRFRLLRLI ENMTFGRAAI GYRAESMHGA GSPQAQRIMI ARTVDFEAKK ELAKNLAGIA
L
//