ID I1VAD0_9CRUS Unreviewed; 367 AA.
AC I1VAD0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
DE Flags: Fragment;
OS Daphnia arenata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=121628 {ECO:0000313|EMBL:AFI39744.1};
RN [1] {ECO:0000313|EMBL:AFI39744.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CC1 {ECO:0000313|EMBL:AFI39744.1};
RX PubMed=22577801; DOI=10.1186/1471-2148-12-63;
RA McTaggart S.J., Obbard D.J., Conlon C., Little T.J.;
RT "Immune genes undergo more adaptive evolution than non-immune system genes
RT in Daphnia pulex.";
RL BMC Evol. Biol. 12:63-63(2012).
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}.
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DR EMBL; JQ856398; AFI39744.1; -; mRNA.
DR AlphaFoldDB; I1VAD0; -.
DR UniPathway; UPA00223; UER01007.
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; 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:SF1; FUMARATE HYDRATASE, MITOCHONDRIAL; 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 2: Evidence at transcript level;
FT DOMAIN 4..286
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFI39744.1"
FT NON_TER 367
FT /evidence="ECO:0000313|EMBL:AFI39744.1"
SQ SEQUENCE 367 AA; 39104 MW; 4E393150160AD928 CRC64;
EVNQDYGLDP KIAASISQAC DEVIDGSLYA DHFPLVIWQT GSGTQSNMNV NEVISNRAIE
IMGGVLGSKK PVHPNDHVNK SQSSNDTYPT AMHIAVAVEV TSNLLPSLQR LHDAIDAKAK
EFQDIIKIGR THTQDATPLT LGQEFSGYAQ QIAFGIERVK ASLPHVYMLA AGGTAVGTGL
NTRIGFAEKV AARVSELTGL PFVTAPNKFE ALASHDALVQ MSGSLNTVAV SLMKIANDIR
FLASGPRCGL GELSLPENEP GSSIMPGKVN PTQCEAITMV AAQVMGNHVA VTIGGSNGHF
ELNVFKPLIV SNVLRSIRLL ADSSNAFTKN SGFGIEANRD RINKLLHESL MLVTALNPHI
GYDKAAK
//
