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Database: UniProt
Entry: A8UW19_9AQUI
LinkDB: A8UW19_9AQUI
Original site: A8UW19_9AQUI 
ID   A8UW19_9AQUI            Unreviewed;       351 AA.
AC   A8UW19;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Reverse gyrase {ECO:0000313|EMBL:EDP75293.1};
DE            EC=5.99.1.3 {ECO:0000313|EMBL:EDP75293.1};
GN   ORFNames=HG1285_00975 {ECO:0000313|EMBL:EDP75293.1};
OS   Hydrogenivirga sp. 128-5-R1-1.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX   NCBI_TaxID=392423 {ECO:0000313|EMBL:EDP75293.1, ECO:0000313|Proteomes:UP000005981};
RN   [1] {ECO:0000313|EMBL:EDP75293.1, ECO:0000313|Proteomes:UP000005981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=128-5-R1-1 {ECO:0000313|EMBL:EDP75293.1,
RC   ECO:0000313|Proteomes:UP000005981};
RA   Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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:EDP75293.1}.
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DR   EMBL; ABHJ01000006; EDP75293.1; -; Genomic_DNA.
DR   RefSeq; WP_008287365.1; NZ_ABHJ01000006.1.
DR   AlphaFoldDB; A8UW19; -.
DR   PATRIC; fig|392423.7.peg.2435; -.
DR   OrthoDB; 9794226at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000005981; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012727; Gly_oxidase_ThiO.
DR   NCBIfam; TIGR02352; thiamin_ThiO; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR13847:SF293; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:EDP75293.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005981}.
FT   DOMAIN          3..329
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   351 AA;  39068 MW;  DF359F5A6B98C94A CRC64;
     MNILIVGSGV VGLSTAFELA LAGHEVRVVT RNYEEGTSWV AGGMLAPFSE GLEGDLLNFS
     IDSLNLYSDF IKRLEEVSRL KLFYVRNGIL RLALGEEEYS FLKGKADLYR RMGYEVEELS
     SEELPEHLSE EPMGGFLFRE EGNVDAEKLM DALLFACENL KVKILIDDIT ELEREGDTIK
     GVKGYRDTYG ADFYVFTAGA WSRSLLKVPV YPVKGQILKV KGLELERVYY STASYIIPKE
     NHILVGATSE DAGFDSRTTL EGIKSLMEGA IRVVPALARS ELLDVRVGFR PATPDEKPVF
     SLGDNFAILT GHYRNGILWA PASANIILEL LEKGKVSKYF EAFSPDRFSS L
//
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