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Database: UniProt
Entry: B8G209_DESHD
LinkDB: B8G209_DESHD
Original site: B8G209_DESHD 
ID   B8G209_DESHD            Unreviewed;       524 AA.
AC   B8G209;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein domain protein {ECO:0000313|EMBL:ACL18532.1};
GN   OrderedLocusNames=Dhaf_0465 {ECO:0000313|EMBL:ACL18532.1};
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL18532.1, ECO:0000313|Proteomes:UP000007726};
RN   [1] {ECO:0000313|EMBL:ACL18532.1, ECO:0000313|Proteomes:UP000007726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
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DR   EMBL; CP001336; ACL18532.1; -; Genomic_DNA.
DR   RefSeq; WP_015942778.1; NC_011830.1.
DR   AlphaFoldDB; B8G209; -.
DR   KEGG; dhd:Dhaf_0465; -.
DR   HOGENOM; CLU_011398_4_6_9; -.
DR   Proteomes; UP000007726; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   PANTHER; PTHR43400:SF12; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..524
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038485036"
FT   DOMAIN          48..490
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   REGION          281..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  55557 MW;  3E6039CE2C979E1A CRC64;
     MTLNRRDFLK KASLGAAVMA GSGFLVGCNT TNVTPPAATP DKWDMETDVV VVGAGNGGLS
     AGAAAAEEGK KVIICEISGF IGGGSIYSGG GLHTWGTKTW EEYKAHTEDL HDPVLAKTYV
     ETFRQTYIPW LQKIGIPITP AGGDRGYLKD YTMGSGEQGY LRQKAYFDAL QKFIEGKGGQ
     ILTNTRVRQL VIDENGAVNG VYAQKKGENP VFIKAGAVVL AAGGFQANKG LTAQYIGSYG
     DTVRNMGTPY NTGSGMLMAQ GVGALTGGSF STFSGTLIGI SPNRQTEENP EEYEKARSGD
     PQTLPGIGNG RPPAPGWVSF LFPEDTTGIL VNLQGKRFMD ETSPIDAKYP RVPQTIIKQK
     RGMALMIADQ AIFDKNKSSD AILKMNESQG VKVIKGNTLD ELATKLQDAY GVYKGTLIKT
     INDYNTAVGN GTAAQLDVPR VGGHFKVAAG PFYAFPTGVA IYHTFGGLII NEKAQVLDLQ
     RQPIANLYAA PPTAAMFREP YAGGIASAGT FGYIAGKVIA KGSV
//
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