ID A0A176J3Z5_9BACI Unreviewed; 491 AA.
AC A0A176J3Z5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=4-hydroxyphenylacetate 3-monooxygenase, oxygenase component {ECO:0000313|EMBL:KZZ83654.1};
GN ORFNames=AS29_015220 {ECO:0000313|EMBL:KZZ83654.1};
OS Bacillus sp. SJS.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423321 {ECO:0000313|EMBL:KZZ83654.1, ECO:0000313|Proteomes:UP000028527};
RN [1] {ECO:0000313|EMBL:KZZ83654.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJS {ECO:0000313|EMBL:KZZ83654.1};
RA Newman J.D., Stropko S.J., Pipes S.E.;
RT "Bacillus sp. SJS genome.";
RL Submitted (APR-2016) 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:KZZ83654.1}.
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DR EMBL; JAQV02000024; KZZ83654.1; -; Genomic_DNA.
DR RefSeq; WP_035409176.1; NZ_JAQV02000024.1.
DR AlphaFoldDB; A0A176J3Z5; -.
DR STRING; 1423321.AS29_015220; -.
DR eggNOG; COG2368; Bacteria.
DR OrthoDB; 9785230at2; -.
DR Proteomes; UP000028527; Unassembled WGS sequence.
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: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 Monooxygenase {ECO:0000313|EMBL:KZZ83654.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000028527}.
FT DOMAIN 5..274
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 282..481
FT /note="HpaB/PvcC/4-BUDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03241"
FT BINDING 104..108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-1"
FT BINDING 150..152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-1"
FT BINDING 156..159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 206..207
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-1"
FT BINDING 455..458
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ SEQUENCE 491 AA; 55448 MW; 100DF6EF30F806D7 CRC64;
MPAKTGKQYI ERVDKAQAEI WIDGEQVKGS ISEHPAFKGV MKSQAELYDM QLDSEKKDYM
TYVSPSSGER VGTSFMKPST KEELVMRRRM MQEWARYNGG MMGRSPDYIN AGLMAYGAAS
EMFGSQDPMY AKNMKNYYEY ARENDLSLTH TLIQPQVNRA VNASQLPDPF IAARIKEKTP
DGVVIKGARL LATQGGITDE IMVFPSTLLK QSEEENPYAY AFCIPNNTPG LKFICRESFD
YGKTSFDHPL GSRFEEMDTI VVFDDVTVPW DRVFSLGDVS VCNQAYNESS AVVHMTHQVV
AKNIAKTEFV LGILQLMAET INIGQYQHIQ EKISEVIIAL ETMKAYVTAS EANANLDRWG
TMTPDFAPLN AARNYFPKIY PRFTEIMQLM GASGLMALPS QADFQSAIRP DLDKYLQSAT
GDAESRVKLY RLAWDVCMSS FGSRQTLYER FFFGDPVRMA SALYTGYDKQ EHVDRVKAFL
DRSEELIKNN G
//
