ID   A0A401HQ12_9EURY        Unreviewed;       242 AA.
AC   A0A401HQ12;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-NOV-2024, entry version 17.
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   Methanofervidicoccus abyssi.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanofervidicoccus.
OX   NCBI_TaxID=2082189 {ECO:0000313|EMBL:GBF36231.1, ECO:0000313|Proteomes:UP000290527};
RN   [1] {ECO:0000313|EMBL:GBF36231.1, ECO:0000313|Proteomes:UP000290527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB {ECO:0000313|EMBL:GBF36231.1,
RC   ECO:0000313|Proteomes:UP000290527};
RX   PubMed=30843780; DOI=.1099/ijsem.0.003297;
RA   Sakai S., Takaki Y., Miyazaki M., Ogawara M., Yanagawa K., Miyazaki J.,
RA   Takai K.;
RT   "Methanofervidicoccus abyssi gen. nov., sp. nov., a hydrogenotrophic
RT   methanogen, isolated from a hydrothermal vent chimney in the Mid-Cayman
RT   Spreading Center, the Caribbean Sea.";
RL   Int. J. Syst. Evol. Microbiol. 69:1225-1230(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-
CC         aspartate + ATP = (2S)-2-[5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamido]succinate + ADP + phosphate + 2 H(+);
CC         Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC         ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000706, ECO:0000256|HAMAP-
CC         Rule:MF_00137};
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 1/2.
CC       {ECO:0000256|ARBA:ARBA00004672, ECO:0000256|HAMAP-Rule:MF_00137}.
CC   -!- SIMILARITY: Belongs to the SAICAR synthetase family.
CC       {ECO:0000256|ARBA:ARBA00010190, ECO:0000256|HAMAP-Rule:MF_00137}.
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:GBF36231.1}.
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DR   EMBL; BFAX01000002; GBF36231.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401HQ12; -.
DR   OrthoDB; 10775at2157; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000290527; Unassembled WGS sequence.
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   FunFam; 3.30.470.20:FF:000006; Phosphoribosylaminoimidazole-succinocarboxamide synthase; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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; IPR050089; SAICAR_synthetase.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   NCBIfam; TIGR00081; purC; 1.
DR   PANTHER; PTHR43599:SF3; BIFUNCTIONAL PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE_PHOSPHORIBOSYLAMINOIMIDAZOLE SUCCINOCARBOXAMIDE SYNTHETASE; 1.
DR   PANTHER; PTHR43599; MULTIFUNCTIONAL PROTEIN ADE2; 1.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00137};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00137};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00137};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00137}; Reference proteome {ECO:0000313|Proteomes:UP000290527}.
FT   DOMAIN          14..238
FT                   /note="SAICAR synthetase/ADE2 N-terminal"
FT                   /evidence="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
//