ID A4WI69_PYRAR Unreviewed; 327 AA.
AC A4WI69;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ABP50086.1};
GN OrderedLocusNames=Pars_0491 {ECO:0000313|EMBL:ABP50086.1};
OS Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=340102 {ECO:0000313|EMBL:ABP50086.1, ECO:0000313|Proteomes:UP000001567};
RN [1] {ECO:0000313|EMBL:ABP50086.1, ECO:0000313|Proteomes:UP000001567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6
RC {ECO:0000313|Proteomes:UP000001567};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000660; ABP50086.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WI69; -.
DR STRING; 340102.Pars_0491; -.
DR KEGG; pas:Pars_0491; -.
DR HOGENOM; CLU_017779_0_1_2; -.
DR OrthoDB; 26910at2157; -.
DR PhylomeDB; A4WI69; -.
DR Proteomes; UP000001567; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
FT DOMAIN 1..171
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 327 AA; 37049 MW; 0DADB9B36B6CBE93 CRC64;
MRPKSVEELV EFINEANRDR RRLLPICRGS KAHLGPPVEY DEELQLWDMP KVLEIDEEEM
VVRTSACISA VELQEELKKR GRRLAVDPPL FRKSSIGGIL STNFYGPMAY RYMTPRDQLL
SVRIVTGKGE FMRYGAPVMK DVAGYNIKRL IAGSWGTLAV LVEAYLRIYA LPDTVAVLAT
SRRALQELRK LYTVGAAEVD GVLYLRFEGV KSEVEYRLSK AGRGDVFYDR EAEEKWGAVT
EAEELFASNE VVKVVAPPAS LPDVQPGVKY LRYPLLGVMY IAGPPPVGVK TYWLKPQRRW
EIENRDLMEK IKQVFDPKGV LSPGRLP
//
