ID A0A0G4B4Y4_9BACT Unreviewed; 442 AA.
AC A0A0G4B4Y4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=phosphoribosylaminoimidazolesuccinocarboxamide synthase {ECO:0000256|ARBA:ARBA00012217};
DE EC=6.3.2.6 {ECO:0000256|ARBA:ARBA00012217};
GN ORFNames=UT28_C0001G0672 {ECO:0000313|EMBL:AKM82468.1};
OS Berkelbacteria bacterium GW2011_GWE1_39_12.
OC Bacteria; Candidatus Berkelbacteria.
OX NCBI_TaxID=1618337 {ECO:0000313|EMBL:AKM82468.1, ECO:0000313|Proteomes:UP000035648};
RN [1] {ECO:0000313|EMBL:AKM82468.1, ECO:0000313|Proteomes:UP000035648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC 4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
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};
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}.
CC -!- SIMILARITY: Belongs to the SAICAR synthetase family.
CC {ECO:0000256|ARBA:ARBA00010190}.
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DR EMBL; CP011213; AKM82468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4B4Y4; -.
DR STRING; 1618337.UT28_C0001G0672; -.
DR KEGG; bbgw:UT28_C0001G0672; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000035648; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR PANTHER; PTHR43599:SF3; BIFUNCTIONAL PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE_PHOSPHORIBOSYLAMINOIMIDAZOLE SUCCINOCARBOXAMIDE SYNTHETASE; 1.
DR PANTHER; PTHR43599; MULTIFUNCTIONAL PROTEIN ADE2; 1.
DR Pfam; PF00731; AIRC; 1.
DR Pfam; PF01259; SAICAR_synt; 1.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 10..273
FT /note="SAICAR synthetase/ADE2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01259"
FT DOMAIN 305..431
FT /note="PurE"
FT /evidence="ECO:0000259|Pfam:PF00731"
SQ SEQUENCE 442 AA; 50044 MW; 577DF738954C591C CRC64;
MIKYEKGEMI SEGKTKQVFK VVGHPGLVII RAKDDITAFD QAKYTKQFPG KGICSTTITC
RVFELLKAAG IPVGYREQLS EREFLAEEGT MIPLEVIGRR CVAPESSCLK RTPQIDPKSI
DPVIRLPRLS VEFDLKTTGG GFIDRFGDRV ELGLNAERKE EDPLIEDPYS QEWQLLHSKK
PAWEDGARLG SVQRDQVISD IALIDKMDDL TRRLFLVLEG MWKMLGYHIL DIKVEYGFNA
RGELMLFDVI DADSWRLRDR KWEDFSKQSF RDGQDLDRVA RKFWIVADKI QQFAIPDQTL
VVWRGSDKDS WPLAPESYED VPNLKIEMVT LSGHKQTGMC LDKLNDLQRD YPSGVILAAV
GMSNGLGPVL AAHSVWPVIG MPATAKEFPE DVWSSLRTPS QTPMLVCLEK NAVNAARNLL
ALQNPVLYMK QQRAVEELDR CA
//
