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Database: UniProt
Entry: L0DCJ8_SINAD
LinkDB: L0DCJ8_SINAD
Original site: L0DCJ8_SINAD 
ID   L0DCJ8_SINAD            Unreviewed;      1450 AA.
AC   L0DCJ8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Putative membrane-bound dehydrogenase {ECO:0000313|EMBL:AGA27104.1};
GN   OrderedLocusNames=Sinac_2812 {ECO:0000313|EMBL:AGA27104.1};
OS   Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS   MOB10).
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Singulisphaera.
OX   NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA27104.1, ECO:0000313|Proteomes:UP000010798};
RN   [1] {ECO:0000313|EMBL:AGA27104.1, ECO:0000313|Proteomes:UP000010798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC   {ECO:0000313|Proteomes:UP000010798};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003364; AGA27104.1; -; Genomic_DNA.
DR   RefSeq; WP_015246254.1; NZ_JH621478.1.
DR   STRING; 886293.Sinac_2812; -.
DR   KEGG; saci:Sinac_2812; -.
DR   eggNOG; COG1413; Bacteria.
DR   eggNOG; COG2133; Bacteria.
DR   eggNOG; COG3828; Bacteria.
DR   HOGENOM; CLU_004500_1_0_0; -.
DR   OMA; YTAWGHD; -.
DR   OrthoDB; 230287at2; -.
DR   Proteomes; UP000010798; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR013427; Haem-bd_dom_put.
DR   InterPro; IPR013428; Membrane-bound_put_N.
DR   InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR   InterPro; IPR029010; ThuA-like.
DR   NCBIfam; TIGR02603; CxxCH_TIGR02603; 1.
DR   NCBIfam; TIGR02604; Piru_Ver_Nterm; 1.
DR   PANTHER; PTHR33546; LARGE, MULTIFUNCTIONAL SECRETED PROTEIN-RELATED; 1.
DR   PANTHER; PTHR33546:SF1; LARGE, MULTIFUNCTIONAL SECRETED PROTEIN-RELATED; 1.
DR   Pfam; PF06283; ThuA; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1450
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003940716"
FT   DOMAIN          1126..1259
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   1450 AA;  157886 MW;  DFF4486BBBBFABDF CRC64;
     MRSMAKQALV VWTFSALFLG SVPFAEAADP LRVLFLGDQG HHRPADRFRQ IDPVLRSRGI
     ELTYSEDVND LNPKTLAGYK AVLLYANIDK IGDDQEQALL DYVNGGGGFV PVHCASYCFR
     NSAKVVALMG AQFLRHGTGV MRDTIAEPDH PLMKGYRGFE SWDETYVHHQ HNTEGRTVLA
     YRVDNQGREP WTWVRTQGKG RVFYTAWGHD ERTWGHPGFE NLLERGIRWA SATDPAVAGA
     FADRSAPPLP TMTPKNPNVK PFEYDEAKIA FYPPDGNPKG DGQWNKMQRP VDPAESQKHI
     IVPEGFTAEL FASEPQIDKP LCMNWDERGR LWIAESVDYP NELKSEGLGR DRIKICEDTD
     GDGRADKFTI FADKLSIPTS LTFSQGGLIV HQAPQTLFLK DNDGDDKADE RRVLFGGWRT
     HDTHAGPSNL RYGLDNWIWG MVGYSGFSGQ VGGEALKFSQ GFYRFKSDGS ALEFLRSTSN
     NSWGVGISEE GLVFGSTANR NPSMYLAIPN RYYEAVRGWS SSVLGMIADT HMFKAVTDRV
     RQVDHHGGYT AGAGHALYTA RAYPEFYWNR TAFVAEPTGH LVGTFVLTRE GSDFHSTNPV
     NLFASDDEWT APTMAEVGPD GQVWVIDWYN YIVQHNPTPA GFATGRGGAY ETDLRDKTHG
     RIYRIVNRAS KLAPPLSLAK ATPGQLVDTL KNSNMFWRIH AQRLLVERGD RDVLPALFAL
     TRDPGVDAIG LNPAAIHALW TIHGLGALDG THPEAAGVAI EALGHKSAGV RMNALKVLPR
     NPQSLEAILT KGLIDDPDAL VRLNALLALS EMPESTGVGK AVAALLMKPE NAGDRWIPDA
     ATAVAARNAL GFLQAVATTK PVSPRLLAVT NIVAEHYARG GPIASVNTLI ASLGDADPSV
     VEAVVAGLVK GWPKDRPATL DEKAEKTLAG VLTRISPGAK GQLLRLATAW GSRHFETYAV
     EVGKSLLADV QDEKQTENQR IATAKQLIGF RPDDSGVVDS LLEIITPRTS PTLAKGIIEA
     LSESRAESVG PALVKLIGRL TPTAKSTAIG VLLRRPVATT ALLNAIENQE VSLGDLTLDQ
     TQSLAAHPEA KIRQRARALL ARGGSLPNAD RQKVIEELSP LVLRKGDAAL GKVVFQQQCL
     KCHTHGAEGG KVGPDLTGMA VHPKEELLVH ILDPSRSVEG NYRQYNVATT DGQVFVGVLT
     SETKTAIELG DAEGKPHVIL RADVEELQAS PKSIMPEGFE KQVNPEGIAN LLEFLTQRGK
     FLPLDLAKSA TIVSTTGMFY SKDAGAERLI FGDWSPKTFE GVPFRLVDPR GERVPNVIML
     FGPAGTFPPT MPKSVSLACN VPAKTIHLLS GVSGWGYPGG AEGSVSMIVR LHYAGGATED
     HPLKNGIHFA DYIRRVDVPE SKYAFPLRGQ QIRYLAITPK RNDVITQIEF VKGPDGTAPV
     VMAVTVEDAE
//
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