ID U6LUZ3_9EIME Unreviewed; 417 AA.
AC U6LUZ3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_03125, ECO:0000256|RuleBase:RU000520};
DE Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_03125};
DE Short=AdSS {ECO:0000256|HAMAP-Rule:MF_03125};
DE EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_03125, ECO:0000256|RuleBase:RU000520};
DE AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_03125};
GN ORFNames=EBH_0043250 {ECO:0000313|EMBL:CDJ51620.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ51620.1};
RN [1] {ECO:0000313|EMBL:CDJ51620.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ51620.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ51620.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ51620.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC nucleotide biosynthesis. {ECO:0000256|RuleBase:RU000520}.
CC -!- FUNCTION: Plays an important role in the salvage pathway for purine
CC nucleotide biosynthesis. Catalyzes the first commited step in the
CC biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_03125}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03125, ECO:0000256|RuleBase:RU000520};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03125};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03125};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03125,
CC ECO:0000256|RuleBase:RU000520}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125}.
CC -!- MISCELLANEOUS: Parasitic protozoa lack the de novo purine biosynthesis
CC pathway and rely exclusively on the salvage pathway for their purine
CC nucleotide requirements. {ECO:0000256|HAMAP-Rule:MF_03125}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_03125, ECO:0000256|RuleBase:RU000520}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03125}.
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DR EMBL; HG712955; CDJ51620.1; -; Genomic_DNA.
DR AlphaFoldDB; U6LUZ3; -.
DR EnsemblProtists; CDJ51620; CDJ51620; EBH_0043250.
DR VEuPathDB; ToxoDB:EBH_0043250; -.
DR OrthoDB; 122722at2759; -.
DR UniPathway; UPA00075; UER00335.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 3.40.440.10; Adenylosuccinate Synthetase, subunit A, domain 1; 2.
DR Gene3D; 1.10.300.10; Adenylosuccinate Synthetase, subunit A, domain 2; 1.
DR Gene3D; 3.90.170.10; Adenylosuccinate Synthetase, subunit A, domain 3; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1.
DR PANTHER; PTHR11846:SF0; ADENYLOSUCCINATE SYNTHETASE; 1.
DR Pfam; PF00709; Adenylsucc_synt; 2.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03125};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03125};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03125};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_03125}.
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT ACT_SITE 100
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 71..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 72..75
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 97..100
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 221
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 235
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 312
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 327
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
SQ SEQUENCE 417 AA; 45948 MW; FD9E67046FCE9CA3 CRC64;
MQPAEPPPPQ QQQQQQQQQQ QEQHEEQQQQ QQQQQQQQQQ QQQQEQEQGR WKLGPCGLSP
QVVCVVGAQW GDEGKGKLVD SLSAAARYCC RFNGGHNAGH KIQIGEKKIT FHILPSGLLQ
PMTIGVLGNG VVIHLKQLIH EMQAAQQILT NTSSSSSSSS SSSSSSSSSR GSSSDKVEVG
KEILSRVLIS SRAHLLFDLH VEVDHREEAA KQQQGAGLGT TLRGVGPCYM TKAARRGLRV
CDILDFDVFT AKYKALARAL EQQFGPLDTN LQQEIEQHRV YRQLLLPCIV DVGFVLRAAL
QKGDTLLLEG ANAALLDLDL GTYPFVTSSN TTAAAACTGL GLSPRCLETV VGVVKAYCTR
VGSGPFPTEL TCGAGDALQQ QQQQQQQQQE QQQQQQQQQE QQQQQQQQQQ QQQQKQQ
//
