ID Q2RJ02_MOOTA Unreviewed; 476 AA.
AC Q2RJ02;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Fumarase {ECO:0000313|EMBL:ABC19587.1};
DE EC=4.2.1.2 {ECO:0000313|EMBL:ABC19587.1};
GN OrderedLocusNames=Moth_1273 {ECO:0000313|EMBL:ABC19587.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC19587.1};
RN [1] {ECO:0000313|EMBL:ABC19587.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC19587.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000232; ABC19587.1; -; Genomic_DNA.
DR RefSeq; YP_430130.1; NC_007644.1.
DR AlphaFoldDB; Q2RJ02; -.
DR STRING; 264732.Moth_1273; -.
DR EnsemblBacteria; ABC19587; ABC19587; Moth_1273.
DR KEGG; mta:Moth_1273; -.
DR PATRIC; fig|264732.11.peg.1366; -.
DR eggNOG; COG1027; Bacteria.
DR HOGENOM; CLU_021594_4_1_9; -.
DR OrthoDB; 9802809at2; -.
DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC.
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:ABC19587.1}.
FT DOMAIN 11..339
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 406..459
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 476 AA; 51349 MW; 724654DF9B138622 CRC64;
MSTRQEHDLL GTREVPATAY YGIHTLRAAE NFNVSRARVH PELIKALATV KEAAARANLD
LGYLPAEKGR AIITACQEVA RGELADQFFL DAYQGGAGTS TNMNVNEVIA NRALEILGRP
KGDYATIHPI DHVNLHQSTN DVYPTAMRVA AIRLLLPLAD ELAKLQEALQ EKEAAFAGVV
KIGRTELQDA VPVTLGQEFG AYAQAISRDR WRLYKVEERL RQVNLGGTAT GTGLNAPLKY
IYLVNDYLRR LTGIGLARAE NMIDATQNMD VFVEVSGLVK AAAVTMHKIA SDLRFMAAGP
RGGPAEINLP ERQAGSSIMP GKVNPVIPEM VSQVAMQVMA NDYLIAMAAS QGQLELNPFA
PLIAHTLLES LAMLAAAARI FRTECITGIT ANPERCQELL AVSPALATAL LPYIGYEKAT
EVVREAVVSG RSIKEIVLEE GYLTSDELEN VLTPAAMTKP GTVGAVKQGI KEKGKA
//
