ID   A0A1H1MXL6_9ACTN        Unreviewed;      1242 AA.
AC   A0A1H1MXL6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:SDR91410.1};
GN   ORFNames=SAMN04489857_1612 {ECO:0000313|EMBL:SDR91410.1};
OS   Parafannyhessea umbonata.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Parafannyhessea.
OX   NCBI_TaxID=604330 {ECO:0000313|EMBL:SDR91410.1, ECO:0000313|Proteomes:UP000199480};
RN   [1] {ECO:0000313|Proteomes:UP000199480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22620 {ECO:0000313|Proteomes:UP000199480};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT629759; SDR91410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1MXL6; -.
DR   OrthoDB; 9804441at2; -.
DR   Proteomes; UP000199480; Chromosome i.
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; cd01740; GATase1_FGAR_AT; 1.
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; 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          182..225
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          433..584
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        1083
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1213
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1215
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1242 AA;  135398 MW;  F8E595169B6A66BB CRC64;
     MVSRVYVEKK PGFDVEAKQL GHELRHTLGV GALTGLRIVN RYDVEGISKS LFEKCILTVF
     SEPQSDVATT RRPAAKGAKV FAVEFLPGQF DQRANSASEC IQLISQGERP TVASAKLYYL
     EGKLTEADVE AIKHYVINPV EAREASLSTR KTLKVDYPKP PMVETLTGFG KLTKRQLQDF
     IDERGLAMDL ADIQFCQKYF KGEKRDPTIT EIKMIDTYWS DHCRHTTFGT QLENVAIDDA
     VVKAAFERYL EVRHELGRDE KPVCLMDMGT IGAKYLKSKG VLKNLDESEE INACTVKVKV
     DVNGKDEDWL FLFKNETHNH PTEIEPFGGA ATCIGGAIRD PLSGRSYVYQ AMRVTGAGDP
     TVPVSETLTG KLPQRKIVRT AAAGYSSYGN QIGLATGQVD ELYHPGYVAK RMEIGAVVGA
     TPASHVRREC PAPGDKIVLL GGRTGRDGIG GATGSSKAHN VESLEKDGAE VQKGNAPTER
     KLQRLFRRED ACRLIKRCND FGAGGVSVAI GELADGLYID LNKVPKKYEG LDGTELAISE
     SQERMAVALA PEDVDEFMRY AHEENLEATV VARVTKEPRL RMVWDGETIC DVSREFLSSN
     GAPKHQDVHV EGQGSYQPDF AGDTLEARMR SVVSDLNVAS NKGLSERFDS TIGAATVLMP
     FGGRYQLTPA MAMVAKLPVF GETTTVSGMA WGFNPYLMSE NQFTGAYLSV VESVAKLAAA
     GIDRKAMYLT FQEYFEKLRD VPERWGKPTA AVLGALMAQL DLGIGSIGGK DSMSGSFEDL
     DVPPTLVSFA TGLGSVDDIV SPEFKRPDSQ LWLVSPTYKA DGVTPDAQSF LKVLDFVHEH
     IGYGVVLSAS TPGYGCLAEQ LFKSAVGNHI GFGLVNEFLA DRLFRLAYGS FVIEVADGTF
     IPTDREGFHV EYLGGTSAEY KMWVEGQELD LAGLQEAWEE GIESVFPYRQ KGEPVKTVTF
     DAAERGVSRP APLVKVPRPR VVIPVFPGNN CEYDSAAAFE RVGAEAKTFI INNLSPEAVA
     ESTDAFVEEV RKSQIIMIPG GFSGGDEPDG SAKFITAFFR APQVTEAVRD LLQARDGLML
     GICNGFQALV KLGLVPFGDI RPMDEKCPTL TFNTIGRHQS RLVRTRVASN LSPWLSQVPV
     GEVDTIAISH GEGRFVASDE LLAQMEAAGQ IATQYVDEDG VPSMDLDVNP NGSVLSIEGI
     TSPDGRVLGK MGHTERSGNG LYKNVPGNKY QKLFEGGVAY FK
//