ID   A0A1N6TE32_9FLAO        Unreviewed;      1231 AA.
AC   A0A1N6TE32;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:SIQ51517.1};
GN   ORFNames=SAMN05880574_11515 {ECO:0000313|EMBL:SIQ51517.1};
OS   Chryseobacterium sp. RU37D.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1907397 {ECO:0000313|EMBL:SIQ51517.1, ECO:0000313|Proteomes:UP000185978};
RN   [1] {ECO:0000313|Proteomes:UP000185978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU37D {ECO:0000313|Proteomes:UP000185978};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FTMM01000015; SIQ51517.1; -; Genomic_DNA.
DR   RefSeq; WP_076446286.1; NZ_FTMM01000015.1.
DR   AlphaFoldDB; A0A1N6TE32; -.
DR   STRING; 1907397.SAMN05880574_11515; -.
DR   OrthoDB; 9804441at2; -.
DR   Proteomes; UP000185978; 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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185978}.
FT   DOMAIN          177..220
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          430..583
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   REGION          445..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1073
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1202
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1204
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1231 AA;  136026 MW;  3A7F2279BBE6E026 CRC64;
     MSQNKRIFVE KRGIFDVESP KIFDEVKAVV PSIQSVKVYN VYDIFGLNDD EFEKVVNSTF
     VDPVTDILIE ENPAKGTHFA LEFLPGQYDQ RADSAQQCIA LLTGNEKSKV RSGKLIEFEG
     VSESDLVKIK DLLINKVESQ EKDLSILDIP AEETPSKVIV HEGFISFDDA QLAEFFNNHG
     FALGLDDLKF IQEYFKSEQR NPTETELKVL DTYWSDHCRH TTFETEFSNI EFEGQFKHTL
     ETIFNDYIEK RKFLGRELKP ISLMDLATVC GRYFHKTGNL DNLVVSDEIN ACTIQIEAEY
     DGKKEPWYLL FKNETHNHPT EIEPFGGAST CLGGAIRDPL SGRSFVFQAM RLTGAADVLE
     SVDKTLPGKL PQKTITKQAA NGYSSYGNQI GLATTMVSEI YDEGYKAKRM EVGFVAGAVP
     VDWVRREKPE AGDSIIILGG ATGRDGVGGA SGSSKEQDET SIHTMSSEVQ KGNAVEERKI
     QRLFRNPEVT RLIKKSNDFG AGGVSVAIGE IADSLEVNLD VLPLKYEGLN GTELAISESQ
     ERMAVVVEPK DKEQFIKFCE AENIVAVEVA KVTDSGRMQM FWKGDKIVDL SRAFLDTNGC
     SKSQEVKITH LNEVKEETPS FNEENFLKIL SDKNVASQKG LLEMFDSSIG ATTVAMPLGG
     KYQQTLMEGS VQTLPIIGAK NIETVSLASW GFDAEISKQN SLLGSSYAVV ESVAKIVAMG
     GDYKNIRFSF QEYFEKLGQN PEKWGKPLAS LLGAYDAQIN FGLAAIGGKD SMSGTYQDLN
     VPPTLISFAC ANGEKKNIIS PEFKGEGNKV YFFNHIAQEN GLPNYDALKT VYEFIFENIK
     AGKIVSVKTV KEGGVAVALA KMSFGNRLGA EITVDDTALL TKNIGSLIIE SKEELSSVNL
     QLIGEVKDSN IIKINDAEFA IKKLLAANAN TFENLFPTVE KEKITVAIDE KLNSINPRNI
     IIKKHGIAQP KVFAPVFPGT NCEYDTLNAF AKEGAVISSL PLININHQLL DESIDAWVEE
     IKTSQILAFS GGFSAGDEPD GSAKFIVNVL KNEKMRNAVH ELLDRDGMII GICNGFQALV
     KSGLLPYGRI KDLDENSPTL AHNAIRRHIS QMVNVRVVND ESPWLKGMKD QVFTIPISHG
     EGRFMASEAE IQKLYENGQI ATQYLDLEGN IAHGMPFNPN NSLFGIEGIT SPDGKIFGRM
     GHPERFAEGL MKNIPTANYH NIFKNGVEYF K
//