ID D2RQE7_HALTV Unreviewed; 477 AA.
AC D2RQE7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ADB62324.1};
GN OrderedLocusNames=Htur_3462 {ECO:0000313|EMBL:ADB62324.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB62324.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB62324.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; CP001860; ADB62324.1; -; Genomic_DNA.
DR RefSeq; WP_012944580.1; NC_013743.1.
DR AlphaFoldDB; D2RQE7; -.
DR STRING; 543526.Htur_3462; -.
DR GeneID; 8744082; -.
DR KEGG; htu:Htur_3462; -.
DR eggNOG; arCOG00337; Archaea.
DR HOGENOM; CLU_018354_10_0_2; -.
DR OrthoDB; 213514at2157; -.
DR Proteomes; UP000001903; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 3: Inferred from homology;
FT DOMAIN 51..221
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 477 AA; 51381 MW; EF532A7D1E36C727 CRC64;
MGTVHKTPGE EALANVPGGA VRSFDAEFAG DVVLPADPEY GRERQVWNGM IDRYPAIVAR
CTGVADVVAA VTFAREQGLP LAVRGGGHNV AGTAVCDGGL VVDLTPMNAV RVDSEERTVR
VEGGATLGDV DRETQLFGLA TALGAVSQTG VAGLTLNGGY GHLSRQYGLA LDNLRSVDVV
TADGQVRTAS AERNADLFWG LRGGGGALGV VTSFEFELHE VGPEVYAFFV WFHADDAAAV
MDRYLEWTAD APREAGVLAF AAHVPALEEF PEETWGEPAV AMLGSYRGDL EDADEVFGAL
RESATPIADL SGTMPYVALQ SMLDEDYPDG LRYYWKSIYL TDVTDEVVDV MLRYNESTPS
ALSTIDLWHL DGAVGEVPPD ATAFRHRDKP YMLTIEANWE DPSGDDANVD WARAAFAEVE
RLPVASGRYG NFPGLNEDPV ERRFGDNYER LVDLKTEYDP TNLFGTTGTV APRTAAD
//
