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Database: UniProt
Entry: A0A109RNU7_9FLAO
LinkDB: A0A109RNU7_9FLAO
Original site: A0A109RNU7_9FLAO 
ID   A0A109RNU7_9FLAO        Unreviewed;       667 AA.
AC   A0A109RNU7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:AMC11484.1};
GN   Name=sdhA {ECO:0000313|EMBL:AMC11484.1};
GN   ORFNames=Lupro_09495 {ECO:0000313|EMBL:AMC11484.1};
OS   Lutibacter profundi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=1622118 {ECO:0000313|EMBL:AMC11484.1, ECO:0000313|Proteomes:UP000059672};
RN   [1] {ECO:0000313|Proteomes:UP000059672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LP1 {ECO:0000313|Proteomes:UP000059672};
RA   Wissuwa J., Le Moine Bauer S., Stokke R., Dahle H., Steen I.H.;
RT   "Complete genome sequence of Lutibacter profundus strain LP1.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMC11484.1, ECO:0000313|Proteomes:UP000059672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LP1 {ECO:0000313|EMBL:AMC11484.1,
RC   ECO:0000313|Proteomes:UP000059672};
RX   PubMed=27118569; DOI=10.1099/ijsem.0.001105;
RA   Le Moine Bauer S., Roalkvam I., Steen I.H., Dahle H.;
RT   "Lutibacter profundi sp. nov., isolated from a deep-sea hydrothermal system
RT   on the Arctic Mid-Ocean Ridge and emended description of the genus
RT   Lutibacter.";
RL   Int. J. Syst. Evol. Microbiol. 66:2671-2677(2016).
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DR   EMBL; CP013355; AMC11484.1; -; Genomic_DNA.
DR   RefSeq; WP_068209305.1; NZ_CP013355.1.
DR   AlphaFoldDB; A0A109RNU7; -.
DR   STRING; 1622118.Lupro_09495; -.
DR   KEGG; lut:Lupro_09495; -.
DR   PATRIC; fig|1622118.3.peg.1962; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000059672; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal 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; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal 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   Reference proteome {ECO:0000313|Proteomes:UP000059672}.
FT   DOMAIN          36..470
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          532..666
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        338
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   667 AA;  74668 MW;  A8B936C36225E273 CRC64;
     MTTLNSRVPE GPIKDKWTLY KDKINLVNPA NKRNIDIIVI GTGLAGGSAA ATLAELGYSV
     KAFAYQDSPR RAHSIAAQGG INASKNYMGD GDSNYRLFYD TVKGGDYRSR EANVYRLAEV
     SGNIIDQCVA QGVPFARDYG GLLDNRSFGG VLVSRTFYAK GQTGQQLLLG AYAAMNRQIA
     RGKIEMFNRH EMLDIVKIDG KARGIIARDL ISGKIERHSA HAVVIATGGY GNVYYLSTNA
     MGSNATAAWK IHKKGAYFAN PCFTQIHPTC IPRSGDYQSK LTLMSESLRN DGRIWVPAKI
     EDAKAIQQGK LKPTEIAEED RDYYLERRYP AFGNLVPRDV ASRAAKERCD AGYGVNATGE
     AVYLDFKAAI HRYGREQAKI HGISNPSEEK IIELGEGIIE AKYGNLFQMY EKIIDENPYK
     TPMMIYPATH YTMGGVWVDY NLMTTVPGLY CIGEANFSDH GANRLGASAL MQGLADGYFV
     LPYTIGDYLS DDIRTGKIAT DTKEFDEVEK EVKDRLEFFI NNKGTHSVDY FHKKLGLVMW
     NKVGMARNEK HLKEAIQEIQ EIREDFWKNV KVPGSLNEFN QELEKAGRVA DFLELGELFA
     KDALEREESC GGHFREEHVT EDGEAKRDDK NYAYVAAWEY TGKPSEAILH KEQLEFKDIE
     LKTRSYK
//
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