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Database: UniProt
Entry: A0A0K0DC11_ANGCA
LinkDB: A0A0K0DC11_ANGCA
Original site: A0A0K0DC11_ANGCA 
ID   A0A0K0DC11_ANGCA        Unreviewed;       488 AA.
AC   A0A0K0DC11;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000804501-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0000804501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   AlphaFoldDB; A0A0K0DC11; -.
DR   STRING; 6313.A0A0K0DC11; -.
DR   WBParaSite; ACAC_0000804501-mRNA-1; ACAC_0000804501-mRNA-1; ACAC_0000804501.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000035642; 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; 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:UP000035642}.
FT   DOMAIN          34..367
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          433..485
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   488 AA;  52868 MW;  027245860385993C CRC64;
     MADEFVLIHV SIHNWVRLNA FVTVPVRKER DTFGELEVPA DKYYGAQTAR SQMNFKIGGP
     EERMPIPVVH AFGILKKAAA IVTVVFIPVI HRETAKMLLP IADEVIQGKL DDHFPLVTWQ
     TGSGTQSNMN VNEVISNRAI EILGGELGSK KPVHPNDHVN MSQSSNDTFP TAMHIAVARE
     INSRLLPALK QLRTSLNNKS VEFKDIIKIG RTHTQDAVPL TLGQEFSGYV QQVDNGIERV
     KAVLPRLYQL AAGGTAVGTG LNTRKGFAEK VAKTVSDITG LPFTTAPNKF EALAAHDALV
     EVHGALNVLA ASFMKIGNDI RFLGSGPRCG LGELSLPENE PGSSIMPGKV NPTQCEAITM
     VAAQVMGNQV AVTVGGSNGH FELNVFKPLM VKNVLQSTRL LADSAVSFSV NCVDGIVANK
     ENIAKIMRES LMLVTALNPH IGYDNAAKIA KTAHKNGTTL KEEAIKLGIL TEEQFAQWVR
     PENMLGPK
//
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