ID   Q38EJ2_TRYB2            Unreviewed;       471 AA.
AC   Q38EJ2;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Adenylosuccinate lyase {ECO:0000256|ARBA:ARBA00017058, ECO:0000256|RuleBase:RU361172};
DE            Short=ASL {ECO:0000256|RuleBase:RU361172};
DE            EC=4.3.2.2 {ECO:0000256|ARBA:ARBA00012339, ECO:0000256|RuleBase:RU361172};
DE   AltName: Full=Adenylosuccinase {ECO:0000256|ARBA:ARBA00030717, ECO:0000256|RuleBase:RU361172};
GN   ORFNames=Tb09.160.5560 {ECO:0000313|EMBL:EAN76778.1};
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431 {ECO:0000313|EMBL:EAN76778.1, ECO:0000313|Proteomes:UP000008524};
RN   [1] {ECO:0000313|EMBL:EAN76778.1, ECO:0000313|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN76778.1,
RC   ECO:0000313|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
RN   [2] {ECO:0007829|PDB:4EFC}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH AMP AND MAGNESIUM.
RA   Wernimont A.K., Loppnau P., Osman K.T., Arrowsmith C.H., Edwards A.M.,
RA   Bountra C., Robinson D.A., Wyatt P.G., Gilbert I.H., Hui R., Lin Y.H.;
RT   "Crystal Structure of Adenylosuccinate Lyase from Trypanosoma Brucei,
RT   Tb427tmp.160.5560.";
RL   Submitted (MAR-2012) to the PDB data bank.
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|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|RuleBase:RU361172};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC       from IMP: step 2/2. {ECO:0000256|ARBA:ARBA00004734,
CC       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|ARBA:ARBA00004706, ECO:0000256|RuleBase:RU361172}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000256|ARBA:ARBA00008273,
CC       ECO:0000256|RuleBase:RU361172}.
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DR   EMBL; CM000207; EAN76778.1; -; Genomic_DNA.
DR   RefSeq; XP_827108.1; XM_822015.1.
DR   PDB; 4EFC; X-ray; 2.00 A; A/B=1-471.
DR   PDBsum; 4EFC; -.
DR   AlphaFoldDB; Q38EJ2; -.
DR   SMR; Q38EJ2; -.
DR   STRING; 185431.Q38EJ2; -.
DR   PaxDb; 5691-EAN76778; -.
DR   GeneID; 3660448; -.
DR   KEGG; tbr:Tb09.160.5560; -.
DR   VEuPathDB; TriTrypDB:Tb927.9.7550; -.
DR   eggNOG; KOG2700; Eukaryota.
DR   InParanoid; Q38EJ2; -.
DR   OMA; NNWAVVA; -.
DR   OrthoDB; 203956at2759; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000008524; Chromosome 9.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0020015; C:glycosome; IDA:GeneDB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:GeneDB.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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   GO; GO:0009152; P:purine ribonucleotide biosynthetic process; TAS:GeneDB.
DR   CDD; cd01598; PurB; 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   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   InterPro; IPR004769; Pur_lyase.
DR   InterPro; IPR047136; PurB_bact.
DR   InterPro; IPR013539; PurB_C.
DR   NCBIfam; TIGR00928; purB; 1.
DR   PANTHER; PTHR43411; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43411:SF1; ADENYLOSUCCINATE LYASE; 1.
DR   Pfam; PF08328; ASL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4EFC};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361172};
KW   Metal-binding {ECO:0007829|PDB:4EFC};
KW   Nucleotide-binding {ECO:0007829|PDB:4EFC};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW   ECO:0000256|RuleBase:RU361172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008524}.
FT   DOMAIN          28..327
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          346..462
FT                   /note="Adenylosuccinate lyase PurB C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08328"
FT   BINDING         29
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         30
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         106
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         107
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         108
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         285
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         289
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         324
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         346
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         348
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         350
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         355
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0007829|PDB:4EFC"
FT   BINDING         359
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0007829|PDB:4EFC"
SQ   SEQUENCE   471 AA;  53120 MW;  B3B15E435CF9DE3E CRC64;
     MEKGSPSDLN GVDYSVDNPL FALSPLDGRY KRQTKALRAF FSEYGFFRYR VLVEVEYFTA
     LCKDVPTIVP LRSVTDEQLQ KLRKITLDCF SVSSAEEIKR LERVTNHDIK AVEYFIKERM
     DTCGLSHVTE FVHFGLTSQD INNTAIPMMI RDAIVTLYLP ALDGIIGSLT SKLVDWDVPM
     LARTHGQPAS PTNLAKEFVV WIERLREQRR QLCEVPTTGK FGGATGNFNA HLVAYPSVNW
     RAFADMFLAK YLGLKRQQAT TQIENYDHLA ALCDACARLH VILIDMCRDV WQYISMGFFK
     QKVKEGEVGS STMPHKVNPI DFENAEGNLA LSNALLNFFA SKLPISRLQR DLTDSTVLRN
     LGVPIGHACV AFASISQGLE KLMISRETIS RELSSNWAVV AEGIQTVLRR ECYPKPYETL
     KKLTQGNTDV TEEQVRNFIN GLTDISDDVR AELLAITPFT YVGYVPRFSA K
//