(data stored in ACNUC7421 zone)

SWISSPROT: C8W2Y3_DESAS

ID   C8W2Y3_DESAS            Unreviewed;       488 AA.
AC   C8W2Y3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 50.
DE   SubName: Full=Fumarate lyase {ECO:0000313|EMBL:ACV61139.1};
GN   OrderedLocusNames=Dtox_0184 {ECO:0000313|EMBL:ACV61139.1};
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:ACV61139.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61139.1, 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; ACV61139.1; -; Genomic_DNA.
DR   RefSeq; WP_015755860.1; NC_013216.1.
DR   STRING; 485916.Dtox_0184; -.
DR   EnsemblBacteria; ACV61139; ACV61139; Dtox_0184.
DR   KEGG; dae:Dtox_0184; -.
DR   eggNOG; COG1027; LUCA.
DR   HOGENOM; HOG000061737; -.
DR   KO; K01744; -.
DR   OMA; RIATIWN; -.
DR   OrthoDB; 734949at2; -.
DR   BioCyc; DACE485916:G1GFV-191-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.10.275.10; -; 1.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR018951; Fumarase_C_C.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   4: Predicted;
DR   PRODOM; C8W2Y3.
DR   SWISS-2DPAGE; C8W2Y3.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Lyase {ECO:0000256|SAAS:SAAS00674282, ECO:0000313|EMBL:ACV61139.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN       12    341       Lyase_1. {ECO:0000259|Pfam:PF00206}.
FT   DOMAIN      407    460       FumaraseC_C. {ECO:0000259|Pfam:PF10415}.
FT   COILED      156    176       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   488 AA;  52707 MW;  B79B7B57137C0EE0 CRC64;
     MTNYRVEKDL LGELKLPRAA YYGINSLRAS QNFAVSGYGV NKHLLRALAE VKLAAAQANL
     QASLLPAETA RAICSAAQEV AEGGLAEQFI VDALQGGAGT STNMNMNEVL ANRAIELLGG
     QKGDYDLVHP LNKVNLSQST NDTYPTALRI AAIRLVLDLS EALAELQTSL QEKEAQFAGI
     LKLGRTELQD ALPITLGQEF GAFAEAIARD RWRLYKVEER LRQINLGGTA IGTGLNAPRR
     YIYQVVEELR QITGLGLARA ENMVDLTQNA DIFAEVSGLV KAAAVNLCKI AGDLMLLAAG
     PAGGLAEINL PPRQAGSSIM PGKVNPVILE AVIQVSWQVM GADQTICQAC AGGRLELNAF
     LPLIAHNLLH VLEMLAKTAR VLNSECIRGI TANEERCRRW LEESNVLVTA LVPYIGYEQA
     TSLAQQAREE NKTIVELVQA RNLLTIEECQ IIAAPRELTR PGIAGARQLA NRFKKANSQG
     DGKNARDT
//

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