SWISSPROT: C8W623_DESAS

ID   C8W623_DESAS            Unreviewed;       315 AA.
AC   C8W623;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 47.
DE   SubName: Full=Sirohydrochlorin cobaltochelatase {ECO:0000313|EMBL:ACV61478.1};
DE            EC=4.99.1.3 {ECO:0000313|EMBL:ACV61478.1};
GN   OrderedLocusNames=Dtox_0558 {ECO:0000313|EMBL:ACV61478.1};
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:ACV61478.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61478.1, 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; ACV61478.1; -; Genomic_DNA.
DR   RefSeq; WP_015756197.1; NC_013216.1.
DR   STRING; 485916.Dtox_0558; -.
DR   EnsemblBacteria; ACV61478; ACV61478; Dtox_0558.
DR   KEGG; dae:Dtox_0558; -.
DR   eggNOG; ENOG4107PPM; Bacteria.
DR   eggNOG; COG4822; LUCA.
DR   HOGENOM; HOG000291079; -.
DR   KO; K02190; -.
DR   OMA; IEACEKR; -.
DR   OrthoDB; 1100154at2; -.
DR   BioCyc; DACE485916:G1GFV-565-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016852; F:sirohydrochlorin cobaltochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019251; P:anaerobic cobalamin biosynthetic process; IEA:InterPro.
DR   InterPro; IPR010388; Anaerobic_Co-chelatase.
DR   Pfam; PF06180; CbiK; 1.
DR   PIRSF; PIRSF033579; Anaer_Co_chel; 1.
PE   4: Predicted;
DR   PRODOM; C8W623.
DR   SWISS-2DPAGE; C8W623.
KW   Cobalt {ECO:0000256|PIRSR:PIRSR033579-3};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Lyase {ECO:0000313|EMBL:ACV61478.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR033579-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    315       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002993394.
FT   ACT_SITE    191    191       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR033579-1}.
FT   METAL       191    191       Cobalt. {ECO:0000256|PIRSR:PIRSR033579-
FT                                3}.
FT   METAL       222    222       Cobalt. {ECO:0000256|PIRSR:PIRSR033579-
FT                                3}.
FT   METAL       254    254       Cobalt. {ECO:0000256|PIRSR:PIRSR033579-
FT                                3}.
SQ   SEQUENCE   315 AA;  35348 MW;  21C1E8D2B73F6669 CRC64;
     MKRAISLSSV ILVLFLLMGC SNTGKQNPTA QNTNPETEKK AILIVSFGTT YEDTRKLTIE
     AVENRAKEEF KGWDVRRAFS SHTIIKVLKE RDGIEVDTPE QALQKLKNDG YTTVVVQMLN
     IIPGVEYDYI KKVVDQYKND NSFKKISCGL PLLYYMGQEN EPNDFITALE ALKTQLPSSM
     KNDEALLVLA HGTPHPANAY YTVLQHTINE LGFKNTYVYT VEGTPTLEEV IPQLKANNIK
     KITLIPFMLV AGDHANNDMA GEEKDSHTSQ LKAEGFAVDS YLHGLGENKE IQNIYMNRIK
     QAMNELNSKP AGEEK
//