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Database: UniProt
Entry: K4KMP0_SIMAS
LinkDB: K4KMP0_SIMAS
Original site: K4KMP0_SIMAS 
ID   K4KMP0_SIMAS            Unreviewed;       743 AA.
AC   K4KMP0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Rieske (2Fe-2S) domain-containing protein {ECO:0000313|EMBL:AFV00445.1};
GN   OrderedLocusNames=M5M_16570 {ECO:0000313|EMBL:AFV00445.1};
OS   Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Simiduia.
OX   NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFV00445.1, ECO:0000313|Proteomes:UP000000466};
RN   [1] {ECO:0000313|EMBL:AFV00445.1, ECO:0000313|Proteomes:UP000000466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC   {ECO:0000313|Proteomes:UP000000466};
RX   PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA   Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT   "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT   bacterium able to degrade a variety of polysaccharides.";
RL   Genome Announc. 1:E00039-E00039(2013).
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DR   EMBL; CP003746; AFV00445.1; -; Genomic_DNA.
DR   RefSeq; WP_015048597.1; NZ_ATUQ01000001.1.
DR   AlphaFoldDB; K4KMP0; -.
DR   STRING; 1117647.M5M_16570; -.
DR   KEGG; saga:M5M_16570; -.
DR   eggNOG; COG2146; Bacteria.
DR   eggNOG; COG2871; Bacteria.
DR   eggNOG; COG3239; Bacteria.
DR   HOGENOM; CLU_021094_0_0_6; -.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000000466; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd03511; Rhizopine-oxygenase-like; 1.
DR   CDD; cd03528; Rieske_RO_ferredoxin; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR039393; Rhizopine-oxygenase-like.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   PANTHER; PTHR43644; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT; 1.
DR   PANTHER; PTHR43644:SF1; NAD(P)H-FLAVIN REDUCTASE; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000466};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        47..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          358..455
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   DOMAIN          466..607
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   743 AA;  84278 MW;  D0D491FFD0B7039E CRC64;
     MSARDYSLTG PCGADAQRNG LADAHWYQSP VDKGAMRALL VRKDWPAIRD TLIWFSLLAV
     AGYSMVQTWG SAWFLLPFFF YAFLYASVSD SRWHECSHGT AFKTDWMNRA LYEVASFMIL
     RESTTWRWSH IRHHTDTIIV GRDPEIASQR PARPLALFLS FFKYPALVTE LRRMLIHACG
     QRDQEAATYV PASEWPAIHW KARVYVAVYV GVVALAIVQQ SWLPLMFVGL PSVFGTWLIG
     LYGYTQHAGL AENVTDHRLN SRTVLMNPLN RFLYWNMNYH VEHHMYPLVP YHALPALHAL
     VKDDCPPAYD GLWAAWKEIL AAWKRQIKDP DYFVRRPLPA PATPAPASEA LAVGHDGWVC
     AGNADQIQNA DVLRIDAAGH TYAIYRNQAG DLFATEGICT HGNAHLAEGL VIGDEIECPK
     HNGRFALSDG HATRAPACVA LERYPVEQRG EKLWLNTAPY PRIDSIRRWS LRVVAVRNLS
     TFIREIELEP QQLVPKFNYQ PGDYLRICVP AYQSLNLNPA QQQGSQSQIW QSLGLHTAKA
     FNRQPCMRNY SLATNPVKDE RLVLNVRLAF NPSAPELHLG VGSGYMYSLS EGDVIEAVGP
     QGEFRIKHTR AEKIYIGGGA GMAPLKSHLS YLLETEQVSQ PIRFWYGARN HQEALYQDYF
     EQLAQKYPNF RFNLVLSEPE SEQDARYPNG FVHQVVEQDF LSKGSDCQQY EFYLCGPPPM
     MAATRNLLQK LGVPEQQIAF DEF
//
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