ID M2MC43_BAUPA Unreviewed; 526 AA.
AC M2MC43;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 08-NOV-2023, entry version 39.
DE RecName: Full=Adenylosuccinate lyase {ECO:0000256|RuleBase:RU361172};
DE Short=ASL {ECO:0000256|RuleBase:RU361172};
DE EC=4.3.2.2 {ECO:0000256|RuleBase:RU361172};
DE AltName: Full=Adenylosuccinase {ECO:0000256|RuleBase:RU361172};
GN ORFNames=BAUCODRAFT_124795 {ECO:0000313|EMBL:EMC94061.1};
OS Baudoinia panamericana (strain UAMH 10762) (Angels' share fungus)
OS (Baudoinia compniacensis (strain UAMH 10762)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Baudoinia.
OX NCBI_TaxID=717646 {ECO:0000313|EMBL:EMC94061.1, ECO:0000313|Proteomes:UP000011761};
RN [1] {ECO:0000313|EMBL:EMC94061.1, ECO:0000313|Proteomes:UP000011761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10762 {ECO:0000313|EMBL:EMC94061.1,
RC ECO:0000313|Proteomes:UP000011761};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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 ECO:0000256|RuleBase:RU361172};
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 ECO:0000256|RuleBase:RU361172};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 2/2. {ECO:0000256|RuleBase:RU361172}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
CC {ECO:0000256|RuleBase:RU361172}.
CC -!- SUBUNIT: Homotetramer. Residues from neighboring subunits contribute
CC catalytic and substrate-binding residues to each active site.
CC {ECO:0000256|ARBA:ARBA00011668}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000256|RuleBase:RU361172}.
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DR EMBL; KB445559; EMC94061.1; -; Genomic_DNA.
DR RefSeq; XP_007679014.1; XM_007680824.1.
DR AlphaFoldDB; M2MC43; -.
DR STRING; 717646.M2MC43; -.
DR GeneID; 19107911; -.
DR KEGG; bcom:BAUCODRAFT_124795; -.
DR eggNOG; KOG2700; Eukaryota.
DR HOGENOM; CLU_030949_1_1_1; -.
DR OMA; ASSCEKI; -.
DR OrthoDB; 460764at2759; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000011761; Unassembled WGS sequence.
DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03302; Adenylsuccinate_lyase_2; 1.
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 InterPro; IPR004769; Pur_lyase.
DR NCBIfam; TIGR00928; purB; 1.
DR PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF10397; ADSL_C; 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 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU361172};
KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW Reference proteome {ECO:0000313|Proteomes:UP000011761}.
FT DOMAIN 417..501
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 526 AA; 59320 MW; BA2F61BE16BE29B6 CRC64;
MSGTTSSRMP DGAGQRMVST PDVRLATLMD MTHLTPTKSA FDAKYDTYQN PLNSRYCSQR
MKYIFSPRNR FSTWRELWIF LAESERELGL EGITTEAIQQ LKDHALIQDH EFETAAIEEK
RRRHDVMAHV HTYGLAAPAA AGIIHWGATS CYVTDNADLI FMRDALDELL PKLAAVIQRF
SAFAKEYRSV PCLGYTHGQA AQMVTVGKRA TIWIEDLLDD LHNLEHARER LLGKFRGVKG
TTGTQASFLA IFQDDHDKVK QLDRLVTKKA GFNGASLSTT QTYSRKIDVD IVHALSSFGC
TCERIGGDIR HLAMFKELEE PFEQDQIGSS AMAYKRNPMR SERLCSIGRM LSSFSAEAEQ
TYKSQWLERS LDDSAIRRIV LPESFLCADA CLILLNNVSS GLVVNEAVIR QRIDLELPFM
ATENIIMEMV TKGHSRQDAH EKIRVLSHQA GAVVKQEGKA NDLIERIRND DFFKPILDDL
KRLMEPETFI GRSPQIVDEV LEIDVKPALA KYEEKLGVVG DAELNV
//
