(data stored in ACNUC7421 zone)

SWISSPROT: C8W2Y1_DESAS

ID   C8W2Y1_DESAS            Unreviewed;       469 AA.
AC   C8W2Y1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   SubName: Full=Biotin and thiamin synthesis associated {ECO:0000313|EMBL:ACV61137.1};
GN   OrderedLocusNames=Dtox_0182 {ECO:0000313|EMBL:ACV61137.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61137.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61137.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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DR   EMBL; CP001720; ACV61137.1; -; Genomic_DNA.
DR   RefSeq; WP_015755858.1; NC_013216.1.
DR   STRING; 485916.Dtox_0182; -.
DR   EnsemblBacteria; ACV61137; ACV61137; Dtox_0182.
DR   KEGG; dae:Dtox_0182; -.
DR   eggNOG; ENOG4105D41; Bacteria.
DR   eggNOG; COG1060; LUCA.
DR   HOGENOM; HOG000287506; -.
DR   KO; K03150; -.
DR   OMA; LICAYRL; -.
DR   OrthoDB; 419725at2; -.
DR   BioCyc; DACE485916:G1GFV-189-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR010722; BATS_dom.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR024007; FeFe-hyd_mat_HydG.
DR   InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR   PANTHER; PTHR43583; PTHR43583; 1.
DR   PANTHER; PTHR43583:SF2; PTHR43583:SF2; 1.
DR   Pfam; PF06968; BATS; 1.
DR   SFLD; SFLDF00319; Fe_hydrogenase_maturase_(HydG-; 1.
DR   SMART; SM00876; BATS; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR03955; rSAM_HydG; 1.
PE   4: Predicted;
DR   PRODOM; C8W2Y1.
DR   SWISS-2DPAGE; C8W2Y1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN       80    301       Elp3. {ECO:0000259|SMART:SM00729}.
FT   DOMAIN      268    380       BATS. {ECO:0000259|SMART:SM00876}.
SQ   SEQUENCE   469 AA;  52976 MW;  FCEA7056DB315E5B CRC64;
     MTVAAADFID DQKIWGLLEE AKNADNKKVK EIIEKAVKAR GLTPGEAAVL LHLEDAALLE
     EMYAAANKIK ESIYGRRLVL FAPLYISNYC VNSCVYCGYR THSKIFRRKL TMDEIKEEVK
     VLEGLGHKRL ALEFGEHPVE CPIDYVLEAI RTIYSVKEKN GSIRRVNVNI AATTVEEYRL
     LKEAGIGTYI LFQETYHRQT YSRMHPAGPK RDYVWHTTAM DRAMQGGIDD VGVGVLFGLY
     DYKYEVMGLL MHALHLEEAF GVGPHTISVP RLKPAAGMDL EQFPHLVSDR DFKKLIAVLR
     LAVPYTGMIL STREGADFRD ELLSIGISQI SAGSCTGVGG YRSQYRQGAG KEEDTRQFNV
     EDNRSPDEVI RSIAESGYIP SFCTACYRQG RTGDRFMALA KTGEIQNVCQ PNAILTFQEF
     LLDYAAPETR IAGDNFIKEQ INQIPDGIIR RKTEEKLEKI KQGWRDLYF
//

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