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Database: UniProt/TrEMBL
Entry: L0GTF9_9GAMM
LinkDB: L0GTF9_9GAMM
Original site: L0GTF9_9GAMM 
ID   L0GTF9_9GAMM            Unreviewed;       460 AA.
AC   L0GTF9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN   ORFNames=Thimo_1235 {ECO:0000313|EMBL:AGA90033.1};
OS   Thioflavicoccus mobilis 8321.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thioflavicoccus.
OX   NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA90033.1, ECO:0000313|Proteomes:UP000010816};
RN   [1] {ECO:0000313|EMBL:AGA90033.1, ECO:0000313|Proteomes:UP000010816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8321 {ECO:0000313|EMBL:AGA90033.1,
RC   ECO:0000313|Proteomes:UP000010816};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA   Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT   "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC       subfamily. {ECO:0000256|ARBA:ARBA00009084}.
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DR   EMBL; CP003051; AGA90033.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0GTF9; -.
DR   STRING; 765912.Thimo_1235; -.
DR   KEGG; tmb:Thimo_1235; -.
DR   PATRIC; fig|765912.4.peg.1197; -.
DR   eggNOG; COG0114; Bacteria.
DR   HOGENOM; CLU_021594_4_1_6; -.
DR   Proteomes; UP000010816; Chromosome.
DR   GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR   GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
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; IPR005677; Fum_hydII.
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; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR11444:SF22; FUMARATE HYDRATASE CLASS II; 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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000010816}.
FT   DOMAIN          2..317
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          383..435
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
FT   REGION          431..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  48108 MW;  03FCF90FD4568FCF CRC64;
     MPLYGEQTRR AVENFAIGGR PMPPSFIHAL GLIKACAARV NGSLGVLPSA TAAAIADAAE
     RVAAGELDGQ FPVDIFQTGS GTSANMNANE VIATLAARAL GEPVHPNDQV NRGQSSNDVI
     PTAIHASAAL ELVGLGSELD ALAESIEQRA AETTDVVKTG RTHLMDAVPL TLGQELGGWA
     AQLRACRARL ADAGVRLRRI AQGGTAVGTG LNADPRFTEA FAAELSRRTG LDFAPAPDAR
     AAIASQDTAV ELSGQLRVLA LALLKVANDL RWMASGPAAG LAEIELPALQ AGSSIMPGKV
     NPVIPEAVAM ACVQVVGLDA AIALAAQDNR FQLCTMLPLI GADLLEQIGL LTRACAALHT
     KAIERFRVNR EGLARTVARN AMLVTALAPM IGYDRAAAIA RRALAEDRAV LDIAREQTTI
     AADELRRLLD PRRLAEPTNG PELSRASGDR AVQEDRQEGD
//
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