ID A0LFT6_SYNFM Unreviewed; 467 AA.
AC A0LFT6;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Fumarate lyase {ECO:0000313|EMBL:ABK16288.1};
GN OrderedLocusNames=Sfum_0589 {ECO:0000313|EMBL:ABK16288.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16288.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK16288.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000478; ABK16288.1; -; Genomic_DNA.
DR RefSeq; WP_011697461.1; NC_008554.1.
DR AlphaFoldDB; A0LFT6; -.
DR STRING; 335543.Sfum_0589; -.
DR KEGG; sfu:Sfum_0589; -.
DR eggNOG; COG1027; Bacteria.
DR HOGENOM; CLU_021594_4_0_7; -.
DR InParanoid; A0LFT6; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000001784; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd01357; Aspartase; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 PANTHER; PTHR42696; ASPARTATE AMMONIA-LYASE; 1.
DR PANTHER; PTHR42696:SF2; ASPARTATE AMMONIA-LYASE; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ABK16288.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT DOMAIN 11..342
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 408..461
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 467 AA; 51233 MW; 9C45AA6E2F3EAE14 CRC64;
MGYRIEKDFL GEKQIPDDVY YGVQTLRGKE NFLITNMPVS KEPNFVKAFG YVKKAAAMAN
RDLGVLDPKI AEAIISACDR IIAGEMLDQF VTDFIQGGAG TSVNMNANEV IANLALESLG
HKKGEYQYVN PNDHVNFGQS TNDVYPTAFH LGLILRLESY MESLGRLRDA FFAKAKEFEN
VLKMGRTHLQ DAVPMSLGQE FHGWGTTVGE EVHRIAEVRQ MLQGVNLGAT AIGTTVTAAP
GYPELAVKYL SELTGIEFTL AEDLIEATSD TGDYVLLSGV IKHTSVKLTK ICNDIRMLAS
GPRCGFGEIN LPQLQPGSSI MPGKVNPVIP EVVNQTGFLV IGLDLTVSLA ASAGQLQLNV
MEPVITFALF ASIMTMQRAV ESLRVNCIEG ITANADRTRD MVLNSLGIVT VLKPSLGYKQ
CAEIAREGFL TEKSLHEIVV NERKLLTQEK WDEVFSFDNL ISPKFEQ
//