ID A0A099P2B8_PICKU Unreviewed; 482 AA.
AC A0A099P2B8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 08-NOV-2023, entry version 37.
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=BOH78_0701 {ECO:0000313|EMBL:ONH76663.1}, BOH78_5363
GN {ECO:0000313|EMBL:ONH70269.1}, C5L36_0A02440
GN {ECO:0000313|EMBL:AWU73640.1}, JL09_g1613
GN {ECO:0000313|EMBL:KGK39183.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK39183.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
RN [2] {ECO:0000313|EMBL:KGK39183.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|EMBL:KGK39183.1};
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for Succinic Acid Production.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000189274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129 {ECO:0000313|Proteomes:UP000189274};
RX PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(2017).
RN [4] {ECO:0000313|EMBL:ONH70269.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129 {ECO:0000313|EMBL:ONH70269.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:AWU73640.1, ECO:0000313|Proteomes:UP000249293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS573 {ECO:0000313|EMBL:AWU73640.1,
RC ECO:0000313|Proteomes:UP000249293};
RA Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT "Population genomics shows no distinction between pathogenic Candida krusei
RT and environmental Pichia kudriavzevii: One species, four names.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; CP028773; AWU73640.1; -; Genomic_DNA.
DR EMBL; JQFK01000011; KGK39183.1; -; Genomic_DNA.
DR EMBL; MQVM01000179; ONH70269.1; -; Genomic_DNA.
DR EMBL; MQVM01000003; ONH76663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099P2B8; -.
DR STRING; 4909.A0A099P2B8; -.
DR VEuPathDB; FungiDB:C5L36_0A02440; -.
DR eggNOG; KOG2700; Eukaryota.
DR HOGENOM; CLU_030949_1_1_1; -.
DR OrthoDB; 460764at2759; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000029867; Unassembled WGS sequence.
DR Proteomes; UP000189274; Unassembled WGS sequence.
DR Proteomes; UP000249293; Chromosome 1.
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, ECO:0000313|EMBL:ONH70269.1};
KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW Reference proteome {ECO:0000313|Proteomes:UP000249293}.
FT DOMAIN 374..458
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 482 AA; 54904 MW; 3DC11C065FE31634 CRC64;
MSQNDSYLTP LSSRYASKEM SHIFSIRNRF STWRKLWYNL AIAEKELGLD IITDEAIAQM
KEHLVITDEE IEAAKIEESK VRHDVMAHVH VFGETCPAAS GIIHLGATSC FVTDNADLIF
LRDAYDILIA KLVNVINRLA KFAYEYKDLP VLGWTHFQPA QLTTVGKRAT LWLQELLWDL
RNFQRARDDL GLRGVKGTTG TQASFLSLFH GNHSKVEELD ERVVELLGFK YAYPCTGQTY
SRKIDIDAIY PLTSFGSSCH KMATDIRLLA NLKEIEEPFE KSQIGSSAMA YKRNPMRSER
VCSLARHLGS LFQDTFQTAS IQWFERTLDD SAIRRISIPE AFLTADILLS TLINITDGLV
VYPKVIERRI KSELPFMATE NIIMAMVEKG GSRQECHEEI RVLSHQASAV VKQQGGDNDL
IERIKNTEYF RPIWNDLDSL LDPSTFIGRA PQQTEKFVNV TVKEALRDYQ KLINDQEVKL
SV
//
