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Database: UniProt
Entry: D2RZY1_HALTV
LinkDB: D2RZY1_HALTV
Original site: D2RZY1_HALTV 
ID   D2RZY1_HALTV            Unreviewed;       545 AA.
AC   D2RZY1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein domain protein {ECO:0000313|EMBL:ADB62678.1};
GN   OrderedLocusNames=Htur_3818 {ECO:0000313|EMBL:ADB62678.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG   Plasmid pHTUR01 {ECO:0000313|EMBL:ADB62678.1,
OG   ECO:0000313|Proteomes:UP000001903}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB62678.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB62678.1, 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};
RC   PLASMID=pHTUR01 {ECO:0000313|EMBL:ADB62678.1,
RC   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};
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DR   EMBL; CP001861; ADB62678.1; -; Genomic_DNA.
DR   RefSeq; WP_012944922.1; NC_013744.1.
DR   AlphaFoldDB; D2RZY1; -.
DR   GeneID; 8744446; -.
DR   KEGG; htu:Htur_3818; -.
DR   HOGENOM; CLU_011398_4_2_2; -.
DR   OrthoDB; 23539at2157; -.
DR   Proteomes; UP000001903; Plasmid pHTUR01.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Plasmid {ECO:0000313|EMBL:ADB62678.1}.
FT   DOMAIN          14..526
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   545 AA;  58451 MW;  DCA659C6A3511F68 CRC64;
     MVANSPEEWD READVVIVGS GGAGLVAALA AESEDILVLE KAASIGGTTA VSGGGLWLPN
     SRPVLEEAGE QPAEQIHAYI RRCAGERVDD ELIETFVELA PDVVDFVESE TALEFQFAGY
     PDYHTDWEEA SDEGNMIEPT LYDGTRLGEN LDDIRDDPHH TFPVPASEIY EAGGHAKFAT
     VADFDELERR NEADLLATGE ALVAGLYEAC LDAGVAFETE APARELVVDD GEVVGVVAAV
     DEEETFVRAG AVVIAAGGMD WDEDMRENFL RGPVTGPATP PQVEGDGIKL GMDVGADLGN
     TNEAWWFPTA HVPGQRWEDG SPLYSMVWGR TLPGSIMVNE DGERFCNEAG NYHDLGKRFH
     TFDPETYEYE NLPAYLVVDS GYREQYSLLT VAPGEEAPDW VAEGETLRDL AVELDVDPDG
     LEATVEAFNE HAREGVDPAF GRGETAYDNF VGDPDTDHPN LAPLNEPPFY AVEVHSGIIG
     TKGGLITRSD GTVLDVDADP IDGLYAASNS TAHVMGMGYA GAGATLGPNV VFGYQAGKHA
     SEFAD
//
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