ID A0A117LKB0_9FIRM Unreviewed; 470 AA.
AC A0A117LKB0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Fumarate lyase {ECO:0000313|EMBL:KUK53546.1};
GN ORFNames=XD78_1121 {ECO:0000313|EMBL:KUK53546.1};
OS Desulfotomaculum sp. 46_296.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1635262 {ECO:0000313|EMBL:KUK53546.1, ECO:0000313|Proteomes:UP000053813};
RN [1] {ECO:0000313|Proteomes:UP000053813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUK53546.1}.
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DR EMBL; LGFZ01000027; KUK53546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117LKB0; -.
DR STRING; 1635262.XD78_1121; -.
DR PATRIC; fig|1635262.3.peg.1758; -.
DR Proteomes; UP000053813; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:amino acid biosynthetic process; 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; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KUK53546.1}.
FT DOMAIN 18..346
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 417..461
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 470 AA; 52054 MW; 6DD7395DA03497B4 CRC64;
MIDPEKESTK RIEHDLIGEK RVPNDAYWGI HTLRAQENFA VSGYRLHPEL IRALCQVKKA
CAQVNIKLEY LDRRVGEAII QACDDIINGS LLDQFLVDVF QGGAGTSTNM NANEVIANRA
LEILGEKKGN YQVIHPNDHV NLHQSTNDTI PTAIRIAMIV LFRNLPIAVT ELINALEDKS
REFKGILKMG RTQHQDAVPL ILGDEFNAYA AVIKRDRTRF LECEDVLSRV NLGGTAIGTG
ITAPKGFGRM AVEMINKNTG LGLAPAGNLI DATQNLDAFA FVSGMLKIHA ANLSKITSDL
MMLHSGPRAG IAEIRLPEVQ AGSSIMPGKV NPVIAEMVEQ VAMRVIANDY VVCEVIRRGR
LELNAFLPLL SHGLFESISI LEKADHIFAS RCIRGITSNE KACREHLELS WKNWGLTALV
PHLGYARCTE LATRAKQMDT TPREIILSEG IFTEDELDQI LFDEQNYSII
//
