ID A0A1Q8AWX9_9CREN Unreviewed; 551 AA.
AC A0A1Q8AWX9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase II {ECO:0000313|EMBL:OLE84232.1};
DE Flags: Fragment;
GN ORFNames=AUF79_17845 {ECO:0000313|EMBL:OLE84232.1};
OS Crenarchaeota archaeon 13_1_20CM_2_51_8.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805093 {ECO:0000313|EMBL:OLE84232.1, ECO:0000313|Proteomes:UP000186073};
RN [1] {ECO:0000313|EMBL:OLE84232.1, ECO:0000313|Proteomes:UP000186073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE84232.1}.
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DR EMBL; MNKD01000798; OLE84232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8AWX9; -.
DR Proteomes; UP000186073; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR CDD; cd02203; PurL_repeat1; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR HAMAP; MF_00420; PurL_2; 1.
DR InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR NCBIfam; TIGR01736; FGAM_synth_II; 1.
DR PANTHER; PTHR43555; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR PANTHER; PTHR43555:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR Pfam; PF00586; AIRS; 2.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 21..57
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 80..192
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 206..354
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 442..541
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT NON_TER 551
FT /evidence="ECO:0000313|EMBL:OLE84232.1"
SQ SEQUENCE 551 AA; 60200 MW; 89D180F7DCFBCFF3 CRC64;
MTRSVIEEPQ SWTLVEVQKP NLTDEEIRYA VKKLQREPNE VEWAMLEAQW SEHCSYKSSK
PLLKRLPSKG PRVLVGPGFD AGVIDIGDGW VVTLHIESHN HPSAIDPYGG AATGVGGVVR
DILSLGTRPI ALLDPLRFGS MDSLHTRWLF DNVVRGIADY GNCIGVPTVG GEVEFDTFFE
RNCLVDVVCV GLGRKDKLVL GEARDPGDLV YLVGGRTGRD GIRGASFASK TLAEKSDTER
SAVQVPDPFT KKLVIEAILE AVDAKIIQGM KDLGGGGLTC GLSEIAAKAG TGIEIDLNRV
QTREPNMQPA EIMISESQER MVLLVREENE RKLVNILNKW EIGYAKIGHV TRDSLLIIRR
GNEVVAKAPA KFVAEAPPVP RSAKRPEYLD ALAEVPEPAM PEDLAQTLIE LLSSPNIASK
EWIYRQYDHE VGIRTIVKPG QADSAILRLP NKRSLALTTG GNSKQCYVDS YWGTVGVVSE
AFCNLVAVGA EPVAAVDHLQ FGNPGNPEVY WTFKEAIRAI ANYLNAVGVP CVGGKVSFYN
EDSMNRRAIK P
//
