ID A0A0V1N0N5_9BILA Unreviewed; 502 AA.
AC A0A0V1N0N5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN Name=fum-1 {ECO:0000313|EMBL:KRZ77575.1};
GN ORFNames=T10_12039 {ECO:0000313|EMBL:KRZ77575.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ77575.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ77575.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ77575.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000256|ARBA:ARBA00004859}.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000256|ARBA:ARBA00009084}.
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:KRZ77575.1}.
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DR EMBL; JYDO01000018; KRZ77575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1N0N5; -.
DR STRING; 268474.A0A0V1N0N5; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000054843; Unassembled WGS sequence.
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:UniProtKB-UniPathway.
DR CDD; cd01362; Fumarase_classII; 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 HAMAP; MF_00743; FumaraseC; 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 NCBIfam; TIGR00979; fumC_II; 1.
DR PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR11444:SF1; FUMARATE HYDRATASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054843}.
FT DOMAIN 50..381
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 447..499
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 502 AA; 54655 MW; 0EE12B4F0525B0F7 CRC64;
MFRVFWQVPK YFSVSSRIQE RIALSQRGIF SWKSYSNMTS DFRIERDTFG ELKVPSDKYY
GAQTARSLMN FDIGGPNERM PLPIIHAFGV LKKAAAIVNK ARGLDAVLSD AIVKAADEVI
EGKLDDHFPL VIWQTGSGTQ SNMNVNEVIS NRAIEILGGQ LGSKNPVHPN DHVNMAQSSN
DTYPTAMHIS TAVEINKLLL PNLKKLHEAL QNKAKEFASI IKIGRTHTQD AVPLSLGQEF
SGYAQQIAYG IERVNATLPR LYELALGGTA VGTGLNTYKG FAEKAAAEIA KQTGLPFKSA
PNKFEALAAH DTMVEVHGAL NVIACSLMKI ANDIRFLGSG PRSGLGELIL PENEPGSSIM
PGKVNPTQCE AVTMVAAQVI GNQVAVSVGG SNGHFELNVF KPLIVSNVLR SIRLISDCSR
SFTDHCVIGI QANHDRIKKL MNESLMLVTA LNPHIGYDKA AQIAKLGHKE GITLKEAALK
LGFLTADQFD QWVKPEEMLG PK
//
