ID   A0A401HQ12_9EURY        Unreviewed;       242 AA.
AC   A0A401HQ12;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-JUL-2019, entry version 3.
DE   RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase {ECO:0000256|HAMAP-Rule:MF_00137};
DE            EC=6.3.2.6 {ECO:0000256|HAMAP-Rule:MF_00137};
DE   AltName: Full=SAICAR synthetase {ECO:0000256|HAMAP-Rule:MF_00137};
GN   Name=purC {ECO:0000256|HAMAP-Rule:MF_00137};
GN   ORFNames=MHHB_P0461 {ECO:0000313|EMBL:GBF36231.1};
OS   Methanococcales archaeon HHB.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales.
OX   NCBI_TaxID=2082189 {ECO:0000313|EMBL:GBF36231.1};
RN   [1] {ECO:0000313|EMBL:GBF36231.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HHB {ECO:0000313|EMBL:GBF36231.1};
RA   Sakai S., Takaki Y., Miyazaki M., Ogawara M., Yanagawa K.,
RA   Miyazaki J., Takai K.;
RT   "Methanofervidicoccus abyssi gen. nov., sp. nov., a hydrogenotrophic
RT   methanogen, isolated from a hydrothermal vent chimney in the Mid
RT   Cayman spreading center, the Caribbean Sea.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate +
CC         ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) +
CC         phosphate; Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58443, ChEBI:CHEBI:77657, ChEBI:CHEBI:456216;
CC         EC=6.3.2.6; Evidence={ECO:0000256|HAMAP-Rule:MF_00137};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00137}.
CC   -!- SIMILARITY: Belongs to the SAICAR synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00137}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GBF36231.1}.
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DR   EMBL; BFAX01000002; GBF36231.1; -; Genomic_DNA.
DR   UniPathway; UPA00074; UER00131.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR   CDD; cd01415; SAICAR_synt_PurC; 1.
DR   HAMAP; MF_00137; SAICAR_synth; 1.
DR   InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR   InterPro; IPR033934; SAICAR_synt_PurC.
DR   InterPro; IPR001636; SAICAR_synth.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   TIGRFAMs; TIGR00081; purC; 1.
DR   PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00137};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00137, ECO:0000313|EMBL:GBF36231.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00137};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00137}.
FT   DOMAIN       14    237       SAICAR_synt. {ECO:0000259|Pfam:PF01259}.
SQ   SEQUENCE   242 AA;  27721 MW;  EE19A2003790C9B1 CRC64;
     MDIDVKEILK REPLYSGKVK SIYEIDEDSV LIEFRDDITA GDGKKRDVKK GKGHLNALIS
     SKLFEVLNKE DIPTHYLGYI DPVYMVAKKV EIIPIEVIVR NIAAGSLCKR YPFKEGEELK
     RPIVQFDYKS DEYGDPMLNE DIAIALGLAT EEELKKLREL ALRVNDTLKR FFDEKGIILV
     DFKIEIGRTK DGHLVVADEI SPDTMRLWDK ETKDVLDKDV FRKDLGDVVS KYEIVAKRIG
     CI
//