ID A0A2T7NZA3_POMCA Unreviewed; 494 AA.
AC A0A2T7NZA3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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 ORFNames=C0Q70_14174 {ECO:0000313|EMBL:PVD26497.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD26497.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD26497.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD26497.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD26497.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) 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:PVD26497.1}.
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DR EMBL; PZQS01000008; PVD26497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7NZA3; -.
DR STRING; 400727.A0A2T7NZA3; -.
DR EnsemblMetazoa; XM_025249485.1; XP_025105270.1; LOC112570839.
DR OrthoDB; 1341425at2759; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg8.
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; 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:UP000245119}.
FT DOMAIN 43..373
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 439..491
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 494 AA; 53442 MW; 3BAC8ACCA3570493 CRC64;
MLHAMLSRLD RGIGSKARQP FSEGAAKIFD KDQYRLEADA FGDIPVPKDK YYGANTARSI
INFAIGDETE RMPIPVIRAF GILKLCAAEV NKEFGLDDRI ANAIIQASKE VISGDLDSHF
PLSTWQTGSG TQTNMNVNEV ISNRAISILG GIIGSKKPVH PNDHVNMSQS SNDTFPTAMH
IAVAQEIENL LKPSLNALCS ALRTKVEAFK DIIKIGRTHL QDAVPLTLGQ EFGAYLHQVQ
TGIERIDATM SHLYELAAGG TAVGTGLNTR VGFAEKVAQR IADYTGLPFV TARNKFEALA
CHDTMVEVHG ALNTLACSLM KIANDIRLLG SGPRCGLAEI SLPENEAGSS IMPGKVNPTQ
CEALTMVAAQ VMGNHVAVSV GASNGHFELN VFKPMIVRNV LQSTRLLADA VISFTRYCVE
GIEANHDNIS ALLKQSLMLV TALNPYIGYD NAAKLATTAH KEGLTLKEAA VRLNLLTEEN
FDHWVKPEDM LGPK
//
