ID D2RYL6_HALTV Unreviewed; 465 AA.
AC D2RYL6;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ADB59917.1};
GN OrderedLocusNames=Htur_1025 {ECO:0000313|EMBL:ADB59917.1};
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:ADB59917.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB59917.1, 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; ADB59917.1; -; Genomic_DNA.
DR RefSeq; WP_012942228.1; NC_013743.1.
DR AlphaFoldDB; D2RYL6; -.
DR STRING; 543526.Htur_1025; -.
DR GeneID; 8741612; -.
DR KEGG; htu:Htur_1025; -.
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 42..213
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 465 AA; 50486 MW; 8D29D3DB4C4CB4F2 CRC64;
MAVHASPVDD NAVSDLQEQF RGTLLRPNDD GYDEARTIWN AMIDRTPAVI TQCEGVADVI
AAVNFGRDHD LPIAVRGGGH NAAGNAVCDD GLVIDLSPMA SVRVDPVAQT ARVGPGATLG
DLDHETLAFG LATPLGFVSE TGVAGLTLGG GFGYLSRKYG MTVDNLRSVD VVTAEGELVH
ASEDEYPDLF WGVRGGGGNF GVVTSFEFDL HEVEPEVLAG LIIHRVEDAP DVIRHWRDFV
ADVPDELTVW VIVLAAPPAS FIPDAYHGST VVAVLPIYLG DLEEGMALIE PLRELGDPVG
DNVEPRSYAA WQQFFDPANA SGARNYWKSL NFTEFPDETI DTCLEYGLTR PTPETKLGLV
HLGGATTRLP ADATAYPHRD AEFVVNITAR WDDPEQDDEC IGWTQEAHDA LAEYSTDGTY
VNFISEQAGE EGFAYGENHD RLVEVKTEYD PENLFRLNQN IEPTA
//
