ID L0DKB6_SINAD Unreviewed; 1748 AA.
AC L0DKB6;
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:AGA29280.1};
GN OrderedLocusNames=Sinac_5128 {ECO:0000313|EMBL:AGA29280.1};
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:AGA29280.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA29280.1, 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; AGA29280.1; -; Genomic_DNA.
DR RefSeq; WP_015248384.1; NZ_JH621480.1.
DR STRING; 886293.Sinac_5128; -.
DR KEGG; saci:Sinac_5128; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG1413; Bacteria.
DR eggNOG; COG2133; Bacteria.
DR eggNOG; COG3474; Bacteria.
DR HOGENOM; CLU_239470_0_0_0; -.
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 GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02795; CBM6-CBM35-CBM36_like; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 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; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR013427; Haem-bd_dom_put.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR013428; Membrane-bound_put_N.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
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; PF00034; Cytochrom_C; 1.
DR Pfam; PF13646; HEAT_2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1748
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003940919"
FT DOMAIN 1454..1587
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 1748 AA; 191653 MW; 74059429354EFF55 CRC64;
MSLRSCLCLL MIVLTTSACQ GEPDAGNRLT YLEEIDPYPV GLKFPKLITP QWVGEDGVEA
VVVLAADDLN ENTALYEAYL RPILDRLKQI DGRAGLSIMT CKANGADPRV QAWLAEGVNL
DVHTLTHPCP LLQKDNLAAA QHEVHGGVDL LNGIRGNKPV AFRMPCCDSQ NTPSPRFYAE
IFNKTSPGRN FLTIDSSVFQ LFTPDDPSLP RELVQDPDGR ERFRKYIPFS SFTNYVENYP
YPYVIGKLCW EFPCSVPSDW EAQHLQQPNN PKTVEDMKAA IDAVVMKQGV FNLVFHPHGW
IKSEQVVELI DHVVAKHGKK VKFLNFREAQ ERLDKNLLGG HPLRASDGRD NGVRVLDVDN
DGYMDVVIGN SKSQLTRIWE PSKKRWSLTK FPGSLVDDGP NGVPQQRGVF GRFDSDGRAA
VIAAFHEHQP AAIQRFVGGG QAVDFVGASA PVDPSTLPAG WERDLQLSQG LEAISGRSTG
LPQGLRLRDL NGDGRCEIIL SNDADNLVLA WSPAQQQGGS TSAWKPLDFR LPPGAQVADR
EGGDGGLRFA DLDEDGYDDL VFSHSPFHKK QADSPATIPD YGLSLFESMT KGWSRDVLKG
QRGDVSALPL IAQAGMNQGM WIHSRHLWWQ NEATAKLPNL VDRRAFNDLL QGVESKAKSP
EASRRSIRVN PGFTVELVAS EPLVEDPIAF DWGADGRLWV LEMGDYPLGR DGKGKAGGVV
RTLEDKDGDG RYDKATLFLD GLAIPSGLLP WRNGVLIACA PDILYVEDRD GDGKADHREV
LFTGFREGNP QHRLNGFELG LDGWVYGANG DSGGEIRSIK TGAIVSINGR DFRFRPDDGR
FEAESGQTQY GRHRDDWGNW FGNSNPIWAW HYVLADSDLR RNPQFAVPDT RQILESDNKL
YPLSRTLARF NEPHSANRVT SANSPTPYRD DLFGRHFESS LFASDPVHNL VHRMILEPDG
ATFLGKRGPD EAEREFLASA DNWTRPTMLK TGPDGALWIA DMYRAVIEHP EWIPDDWEAK
LDLRAGSEQG RIYRVFPVEK RPRPITRLDR FDTVGLVAAL DSPNGWQRDT AQRLLLHKGD
RAAAGPLRDL AAKSSRPKTR LQALWTLQTL EELTVPAVIG ALSDPHPQVR RNAIKAGSVL
LKSAPELGEA MLRLTGDPDP QVRFQLALSL GDWSDPRAGR ALATLIQRDP NDRWLRAAVL
SSAAPHVGSI IAALFENAKD EAPSTAILDP LFALAATAKE REGLASLVET LSTPAGQGGQ
FAPWQFSALA SLLDASVRAR KPVAEADLKR FEKIREAARA LAGDDKAGEE DRLAAVRLLG
RDKESQSLDR PRLVGLLRPQ VSGALQQAAV AALSRGDDPQ VPTILIDGWK GHSPQLRTAI
LDTLLSRDPW TKILLFSLED TCLPPAEIGP THRRRLLSHR DAALKARAEA VFSRETSTRQ
EVIAAYQTAT TLPGNAATGA ALFKKVCATC HRVGQEGAEV GPDLAALTDK SPGALLVAIL
DPNRALEAKY ANFTVQTTDG RVLTGLIASE TATAVTLRRQ EGKEDVLLRA EIDEIAASGQ
SLMPEGLEKD LKPQDVADLL AFLGAVGPPP KQVEGNRPER VTPGADGTIA LRAETAELYG
DTLTFEAKHK NLGYWGRPSD RAVWKFVSER PGRYRVWIDW ACDNDSAGNS LLLELGSQRL
EHPVTGTGDW DTYQSADIGE VTLTPGAHRL ELHSAGPVKG ALLDLRSVEL RPVPDPAKPT
TPGSCCNP
//
