ID E1R540_SEDSS Unreviewed; 466 AA.
AC E1R540;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Fumarate lyase {ECO:0000313|EMBL:ADK80575.1};
DE EC=4.2.1.2 {ECO:0000313|EMBL:ADK80575.1};
GN OrderedLocusNames=Spirs_1448 {ECO:0000313|EMBL:ADK80575.1};
OS Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
OS (Spirochaeta smaragdinae).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Sediminispirochaeta.
OX NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK80575.1, ECO:0000313|Proteomes:UP000002318};
RN [1] {ECO:0000313|EMBL:ADK80575.1, ECO:0000313|Proteomes:UP000002318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228
RC {ECO:0000313|Proteomes:UP000002318};
RX PubMed=21304743; DOI=10.4056/sigs.1143106;
RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., Nolan M.,
RA Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N.,
RA Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Rohde M.,
RA Brambilla E., Spring S., Goker M., Sikorski J., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT 4228).";
RL Stand. Genomic Sci. 3:136-144(2010).
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DR EMBL; CP002116; ADK80575.1; -; Genomic_DNA.
DR RefSeq; WP_013254039.1; NC_014364.1.
DR AlphaFoldDB; E1R540; -.
DR STRING; 573413.Spirs_1448; -.
DR KEGG; ssm:Spirs_1448; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_12; -.
DR Proteomes; UP000002318; Chromosome.
DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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:ADK80575.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002318}.
FT DOMAIN 16..344
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 410..462
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 466 AA; 50390 MW; ED1204FE029F0B78 CRC64;
MESKKGFRIE KDSMGEMLVP EHVYWGAQTA RAVKNFTVSS RRIPEGLRLA LGWIKEGAAV
AHGELGTFPE AVCDAVEEAA RELRRGKFAD QFPIDLYQTG SGTSWNMNAN EVVAARANEL
LGFPLGSRGP VHPNDTVNRG QSSNDVIPSA IQIASRLSAK CLARDLRYLA EAVETKAEES
RDVIKLGRTH LQDAVPMTGF QELSAWADQL HQALRRLKAL FPVLERIPLG GTAVGTGLNS
SRNFADLTAT HIAEGTGCPF VAMDRSFSAI AARDASLEYG DVLNALAVII MKIAQDLRLL
SSGPRAGLAE IRLPELQPGS SIMPGKVNPV IPEMAVQVAA SVMGKHVSLT IACQNSPLQL
NIMMPLIAGE LLDSAEMLSR LCRSLADRCI SGMSYDRQRC RDLIEGSLAM VTPLALEIGY
EKAARIAKEA YASGRNVREV ALKQSGLDSE TVQRLLDPER MCGGVD
//
