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
//