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Database: UniProt
Entry: A0A1I4XAN0_9FLAO
LinkDB: A0A1I4XAN0_9FLAO
Original site: A0A1I4XAN0_9FLAO 
ID   A0A1I4XAN0_9FLAO        Unreviewed;      1236 AA.
AC   A0A1I4XAN0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:SFN22991.1};
GN   ORFNames=SAMN05421738_108185 {ECO:0000313|EMBL:SFN22991.1};
OS   Algoriella xinjiangensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Algoriella.
OX   NCBI_TaxID=684065 {ECO:0000313|EMBL:SFN22991.1, ECO:0000313|Proteomes:UP000199149};
RN   [1] {ECO:0000313|EMBL:SFN22991.1, ECO:0000313|Proteomes:UP000199149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XJ109 {ECO:0000313|EMBL:SFN22991.1,
RC   ECO:0000313|Proteomes:UP000199149};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOUZ01000008; SFN22991.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4XAN0; -.
DR   STRING; 684065.SAMN05421738_108185; -.
DR   OrthoDB; 9804441at2; -.
DR   Proteomes; UP000199149; 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; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 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   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}.
FT   DOMAIN          177..225
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          435..587
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        1077
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1206
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1208
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1236 AA;  138382 MW;  DC4241687D7F39B5 CRC64;
     MNQRLFIQKK SNFDIISQKT TIELKNLVPT IVCKVFVIYD LFNIDENQLQ EVQNKVFVDP
     VTDNVYKHLS DTLNYSFPDT KNYFATEFLP GQYNQRDDSS EQCLVLMNVE NVTVKSGLLY
     VFNNDLTEQD LQKVKDYLIN PIESRVKDLS KMEIPANPEA TEVPTIENFI STDQKGLEEI
     YKTYGLSLEM DDLVFIQDYF KSIQRNPTET ELKVLDTYWS DHCRHTTFET EITDIKFNSK
     FNTTLQKTFD YYQQIRQELG ITKPIRLMDL ATIMGKYLSR TGVVTNIDVS EEINACSIVV
     PIDVDGIEEE WLLQFKNETH NHPTEVEPFG GASTCVGGAI RDPLSGRSYV FQAMRITGAA
     NPLEKIEDTL PGKLAQRKIS KEAANGYSSY GNQIGLATTF VKEIYDEGYK AKRMEVGFVA
     GAVKKEYVRR EEPVAGDRII LLGGATGRDG VGGASGSSKT HDGLKLDDLS AEVQKGNAIV
     ERKIQRLFRN PEVLALIKKC NDFGAGGVSV AIGEIARGIN VDLDKVPLKY AGLNGTELAI
     SESQERMAVA VEAKDVDTFI ALAKEENLEA TCVAEVTEDD TMTLVWKGTK IVELDRKFLD
     TNGVRKQSKI EVTDEEYKNP FENKSFDKNE FIAMMQELNH ASQKGMVEMF DNNVGRSTIL
     NAFGGKTMDT PEDVSVQKFP TDGFTNAVSI AAYGFSPQIS RWSNYHGGYF AVIDSMTKIV
     AAGGNYADIR LTFQEYFEKL RDEATRWGKP FSALLGTIEA QRQFGIPAIG GKDSMSGSYQ
     DIDVPPTLIS FAVAPSQANK IVQGTLAEKN SKLSVFVPTQ NEDYLLDETN VKAIFDFITS
     LNQENVKSMM TVKFGGIAET LANMAFGNEI GFAINTTLDL AKYYPGSIII EHTEDLTIPT
     EITQNYHVLG ETNNSVNISF NGDEINLNEL KQQWKETFNS LFPYQSNSEE IVEEKDLKVE
     QICFAFADHK VENPKVFIPI FPGTNSEYDS AKAFRREGAI VKTLPFRNLT QQDVEESVEE
     FVKEINQANI FFIPGGFSAA DEPDGSGKFI ATVLRNEKIK NAIHQLLERD GLILGVCNGF
     QGLIKSGLLP YGKIQELEEN TPTLTFNEIG RHITQLAQVR VNKSHSPWLK GMENQTYWIP
     FSHGEGRFVA NDFELEKLID KGQIATQFID LEGKLAGQMP YNPNGSTFAV EGIVSPCGKI
     YGRMGHPERY EEGLFKNIPG NGSMNIFKNA VEYFRN
//
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