ID A0A0K0D9Y8_ANGCA Unreviewed; 465 AA.
AC A0A0K0D9Y8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=ADSL_C domain-containing protein {ECO:0000313|WBParaSite:ACAC_0000700901-mRNA-1};
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_0000700901-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_0000700901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- FUNCTION: Catalyzes two non-sequential steps in de novo AMP synthesis:
CC converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole-4-carboxamide, and thereby also contributes to de
CC novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP)
CC to AMP and fumarate. {ECO:0000256|ARBA:ARBA00002971}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
CC carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide + fumarate; Xref=Rhea:RHEA:23920,
CC ChEBI:CHEBI:29806, ChEBI:CHEBI:58443, ChEBI:CHEBI:58475; EC=4.3.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000598};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate;
CC Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567,
CC ChEBI:CHEBI:456215; EC=4.3.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000811};
CC -!- SUBUNIT: Homotetramer. Residues from neighboring subunits contribute
CC catalytic and substrate-binding residues to each active site.
CC {ECO:0000256|ARBA:ARBA00011668}.
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DR AlphaFoldDB; A0A0K0D9Y8; -.
DR STRING; 6313.A0A0K0D9Y8; -.
DR WBParaSite; ACAC_0000700901-mRNA-1; ACAC_0000700901-mRNA-1; ACAC_0000700901.
DR Proteomes; UP000035642; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR Gene3D; 1.10.275.60; -; 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 InterPro; IPR019468; AdenyloSucc_lyase_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; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000035642}.
FT DOMAIN 363..442
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 465 AA; 53223 MW; 63C19073912D30E7 CRC64;
MDAECCYESV LASRYCKSSP LVQILSERNK TILWRQLWIW LAEAQLELGL KQVTPEAIEE
MKQKRDCIDW HKIREEERRL KHDVMAHNHA FGAICPRAAG IIHLGATSCY VQDNADIIVI
RESVNQILRR AAIVLDRMAK FAEREKSHVT VGRTHYQTAS LVTIGKRTAL WAQELLMGFK
ELERFHDTMK FRGIKGATGT QDSFLTLFGG DEEMVEKLDD LVTSKAGFSQ KFLISGQTYS
RQQKSFWLTT GCPFDIRARC HCEHFYQDQI GSSAMPYKKN PMKSERCCSL ARKLIHTPQE
ALSILGDQGL ERTLDDSAGR RILLPDSLLT AEAMLTTLQN VFEGLTVQTE NVARVVREEL
PFLGLEKAMM WLTEEGVDRQ QAHSVIRTTA LEAKERQTKE VVQMSDVLRD PFFNSVRDRV
MALVDEPIRF TGRCESQTVR FITEELRPTI DRYFDPNAAE VQLNV
//
