ID A0A139PB14_9STRE Unreviewed; 430 AA.
AC A0A139PB14;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
DE Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_00011};
DE Short=AdSS {ECO:0000256|HAMAP-Rule:MF_00011};
DE EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
DE AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00011};
GN Name=purA {ECO:0000256|HAMAP-Rule:MF_00011};
GN ORFNames=STRDD11_00459 {ECO:0000313|EMBL:KXT85257.1};
OS Streptococcus sp. DD11.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777879 {ECO:0000313|EMBL:KXT85257.1, ECO:0000313|Proteomes:UP000070514};
RN [1] {ECO:0000313|EMBL:KXT85257.1, ECO:0000313|Proteomes:UP000070514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD11 {ECO:0000313|EMBL:KXT85257.1,
RC ECO:0000313|Proteomes:UP000070514};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC nucleotide biosynthesis. Catalyzes the first committed step in the
CC biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
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_00011, ECO:0000256|RuleBase:RU000520};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00011};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00011};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00011,
CC ECO:0000256|RuleBase:RU000520}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00011}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXT85257.1}.
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DR EMBL; LQRF01000056; KXT85257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139PB14; -.
DR STRING; 1777879.STRDD11_00459; -.
DR PATRIC; fig|1777879.3.peg.511; -.
DR OrthoDB; 9807553at2; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000070514; Unassembled WGS sequence.
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; 1.
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; IPR033128; Adenylosuccin_syn_Lys_AS.
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 NCBIfam; TIGR00184; purA; 1.
DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1.
DR PANTHER; PTHR11846:SF0; ADENYLOSUCCINATE SYNTHETASE; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00011};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00011};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00011};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00011};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00011};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00011}.
FT ACT_SITE 13
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT ACT_SITE 41
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT ACT_SITE 139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10134"
FT BINDING 12..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 13..16
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 38..41
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 40..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 128
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 142
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 223
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 238
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 298..304
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 302
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 304
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 330..332
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT BINDING 412..414
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
SQ SEQUENCE 430 AA; 47746 MW; C316B919C8EA0011 CRC64;
MTSVVVVGTQ WGDEGKGKIT DFLSANAEVI ARYQGGDNAG HTIVIDGKKY KLHLIPSGIF
FPEKISVIGN GMVVNPKSLV KELAYLHGEG ITTDNLRISD RAHVILPYHI ELDRLQEEAK
GEHKIGTTIK GIGPAYMDKA ARVGIRIADL LDRDIFRERL ERNLAEKNRL FEKLYDSRAM
SVEDIFEEYY AYGQQIKQYV TDTSVILNDA LDHGKRVLFE GAQGVMLDID QGTYPFVTSS
NPVAGGVTIG SGVGPSKIDK VVGVCKAYTS RVGDGPFPTE LFDEIGDRIR DVGHEYGTTT
GRPRRVGWFD SVVMRHSRRV SGITNLSLNS IDVLTGLDTV KICVAYDLDG QRIDHYPASL
EQLKRCRPIY EELPGWQEDI TGVRSLEDLP ENARNYVRRV SELVGVRIST FSVGPGREQT
NILESVWSSL
//
