ID   A0A1M6U7P8_9FLAO        Unreviewed;      1230 AA.
AC   A0A1M6U7P8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:SHK65098.1};
GN   ORFNames=SAMN05444371_3179 {ECO:0000313|EMBL:SHK65098.1};
OS   Epilithonimonas mollis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Epilithonimonas.
OX   NCBI_TaxID=216903 {ECO:0000313|EMBL:SHK65098.1, ECO:0000313|Proteomes:UP000184498};
RN   [1] {ECO:0000313|Proteomes:UP000184498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18016 {ECO:0000313|Proteomes:UP000184498};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FRAM01000004; SHK65098.1; -; Genomic_DNA.
DR   RefSeq; WP_072999906.1; NZ_FRAM01000004.1.
DR   AlphaFoldDB; A0A1M6U7P8; -.
DR   STRING; 216903.SAMN05444371_3179; -.
DR   OrthoDB; 9804441at2; -.
DR   Proteomes; UP000184498; Unassembled WGS sequence.
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:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd02203; PurL_repeat1; 1.
DR   CDD; cd02204; PurL_repeat2; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR010141; FGAM_synthase.
DR   InterPro; IPR041609; PurL_linker.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   NCBIfam; TIGR01857; FGAM-synthase; 1.
DR   PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   Pfam; PF18072; FGAR-AT_linker; 1.
DR   Pfam; PF13507; GATase_5; 1.
DR   SMART; SM01211; GATase_5; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT   DOMAIN          174..218
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          430..581
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   REGION          443..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1230 AA;  136047 MW;  8EDB158871083FC0 CRC64;
     MNKRIFVEKR GIFDVESPKI FDEVKAVIPS IQKVKVYNVY DIFGLNGGEF EKVVNSTFVD
     PVTDILIEEN PAKGTHFALE FLPGQYDQRA DSAQQCIALL TGNEQSKVRS GKLIEFEGVS
     ESDLVKIKDL LINKVESQEK DLSILDIPEE ETPSKVIVHE GFINFDDAQL EEFFNNHGFA
     LGLDDLKFIQ EYFKSEQRNP TETELKVLDT YWSDHCRHTT FETELSNIEF EGHFKHTLET
     IFNDYIEKRK FLGRELKPIS LMDLATVCGR YFHKTGNLEN LVVSDEINAC TIQIETEYDG
     KKEPWYLLFK NETHNHPTEI EPFGGASTCL GGAIRDPLSG RSFVFQAMRL TGAADVLEPV
     DKTLPGKLPQ KTITKQAANG YSSYGNQIGL ATTMVSEIYD EGYKAKRMEV GFVAGAVPVD
     WVRREKPANG DSIIILGGAT GRDGVGGASG SSKEQDETSI HTMSSEVQKG NAVEERKIQR
     LFRNPEVTRL IKKSNDFGAG GVSVAIGEIA DSLEVNLDVL PLKYEGLNGT ELAISESQER
     MAVVVEPKDK EKFIKFCEAE NIVAVEVAKV TDSGRMQIFW KGDKIVDLSR AFLDTNGCSK
     SQEVKITHLN EVKEEAPAFN EENFLKILSD KNVASQKGLL EMFDSSIGAT TVAMPLGGKY
     QQTLMEGSVQ TLPILGAKDI ETVSLASWGF DAEISKQNSL SGASYAVVES VAKIVAMGGD
     YKNIRFSFQE YFEKLGQNPE KWGKPLASLL GAYDAQINFG LAAIGGKDSM SGTYQDLNVP
     PTLISFACAN GEKKNIISPE FKQAGNKLYF FNHIPQENGL PNYNTLKNIY EFIFENIKAG
     KIVSVKTVKE GGVAVALAKM SFGNRLGADI TVDDASALLS KRVGSLIIES KEELSSVNLQ
     LIGQVVANEV LTINNLQTSI NKLLAGNTNT FENLFPTVEK EKITVALDEK LNSVNPRNII
     LKKHKIAQPR VFAPVFPGTN CEYDTLNAFA KEGAIVNSLP FKNINHQVLD ESIDAWVEEI
     KQSQILAFSG GFSAGDEPDG SAKFIVNVLK NEKMRTAVHE LLDRDGMIIG ICNGFQALLK
     SGLLPYGKIK DLDENSPTLA HNAIRRHISQ MVNVKVLNDE SPWLKGMKDQ VYTIPISHGE
     GRFMASEAEI KNLYENGQIA TQYLDLEGNI AHGMPFNPNN SLFGIEGITS PCGKIFGRMG
     HPERFAEGLF KNIPTANYHN IFKNGVEYFK
//