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Database: UniProt
Entry: A0A063Y590_9GAMM
LinkDB: A0A063Y590_9GAMM
Original site: A0A063Y590_9GAMM 
ID   A0A063Y590_9GAMM        Unreviewed;      1300 AA.
AC   A0A063Y590;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000256|HAMAP-Rule:MF_00419};
DE            Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00419};
DE            Short=FGAMS {ECO:0000256|HAMAP-Rule:MF_00419};
DE            EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00419};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419};
DE            Short=FGAR amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419};
DE            Short=FGAR-AT {ECO:0000256|HAMAP-Rule:MF_00419};
GN   Name=purL {ECO:0000256|HAMAP-Rule:MF_00419};
GN   ORFNames=ADINL_0498 {ECO:0000313|EMBL:KDE40849.1};
OS   Nitrincola lacisaponensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Nitrincola.
OX   NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE40849.1, ECO:0000313|Proteomes:UP000027318};
RN   [1] {ECO:0000313|EMBL:KDE40849.1, ECO:0000313|Proteomes:UP000027318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4CA {ECO:0000313|EMBL:KDE40849.1,
RC   ECO:0000313|Proteomes:UP000027318};
RX   PubMed=16280482; DOI=10.1099/ijs.0.63647-0;
RA   Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A.,
RA   Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.;
RT   "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic
RT   bacterium isolated from an alkaline, saline lake.";
RL   Int. J. Syst. Evol. Microbiol. 55:2273-2278(2005).
CC   -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC       purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC       formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC       formylglycinamidine ribonucleotide (FGAM) and glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC         ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC         ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC         ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00419};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00004920, ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC       {ECO:0000256|ARBA:ARBA00008608, ECO:0000256|HAMAP-Rule:MF_00419}.
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:KDE40849.1}.
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DR   EMBL; JMSZ01000015; KDE40849.1; -; Genomic_DNA.
DR   RefSeq; WP_036543628.1; NZ_JMSZ01000015.1.
DR   STRING; 267850.ADINL_0498; -.
DR   PATRIC; fig|267850.7.peg.492; -.
DR   OrthoDB; 9804441at2; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000027318; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 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   HAMAP; MF_00419; PurL_1; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR040707; FGAR-AT_N.
DR   InterPro; IPR010073; PurL_large.
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   InterPro; IPR036604; PurS-like_sf.
DR   NCBIfam; TIGR01735; FGAM_synt; 1.
DR   PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   Pfam; PF02769; AIRS_C; 2.
DR   Pfam; PF18072; FGAR-AT_linker; 1.
DR   Pfam; PF18076; FGAR-AT_N; 1.
DR   Pfam; PF13507; GATase_5; 1.
DR   SMART; SM01211; GATase_5; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR   SUPFAM; SSF82697; PurS-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00419}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00419};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00419};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00419};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00419};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00419};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00419}; Reference proteome {ECO:0000313|Proteomes:UP000027318}.
FT   DOMAIN          35..150
FT                   /note="Phosphoribosylformylglycinamidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18076"
FT   DOMAIN          171..220
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          432..588
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          838..971
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   REGION          306..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1140
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1265
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1267
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         307..318
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         386..388
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         678
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         679
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         718
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         722
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         886
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         888
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ   SEQUENCE   1300 AA;  141049 MW;  96DE71BED4D00B96 CRC64;
     MLVLRGAPAL STFRHDKLLS LLQAQVSQVT GLYAEFVHFA EAQAPLDADA EAVLERILSY
     GPKGRVENPD GQLFLVMPRP GTISPWSSKA TDIAHNCGLT QINRLERGLA YYIHSETALD
     ADASQVIAAL LHDRMTQMVA ASMADASSLF RHESPRALGH VDVLQGGRAA LESANQTLGL
     ALADDEIDYL LRSFIELQRN PTDVELMMFA QANSEHCRHK IFNASWDIDG EAQDKSLFAM
     IRNTNEVAGD NVLSAYKDNA AVIRGSDAGR FYPDPDTAAY GYHQEPIHIL MKVETHNHPT
     AIAPHPGAAT GSGGEIRDEG ATGKGAKPKA GLTGFSVSDL NIPGFEQPWE SSYGKPERIV
     TALDIMLEGP IGGAAFNNEF GRPNLTGYFR TFEQSVPGAA GEEVRGYHKP IMIAGGMGNI
     RESHVEKGEI PVGAKLICLG GPAMLIGLGG GAASSMTSGS SAADLDFASV QRDNPELERR
     CQEVIDRCWQ LGDRNPIAFI HDVGAGGLSN AFPELVKDGG RGGHFELRNI NNDEPGMSPL
     EIWCNEAQER YVLAVTPEDM PRFEAICARE RCPYAVVGEA IDEQHLTLND QHFDTRPVDL
     PMSVLFGKPP KMHRSVSRIN YEVPAFDAAD IELEEAVERV LKLPAVASKS FLITIGDRTI
     TGLVARDQMV GPWQVPVADC AVTAASFDTY AGEAMAMGER TPLALIDSPA SGRMAIGETL
     TNIAAARIAD IRDVKLSANW MCAAGHPGED EKLYDTVHAV GMELCPALGI TIPVGKDSMS
     MRTVWQQDGE DKSVTAPMSL IISGFAPVVD VRKTLTPQLV VDQGETDLLL IDLGAGQNRL
     GLSALAQVYN QVGQTVPDLD DADQMVAFFT AIQELNAQGL ILAYHDRSDG GLFVTLAEMA
     FAGHCGIDVN LDMLASSLDE VPAALFAEEL GAVLQVRREV TEQVLTELNA AGLSECVCVI
     GSVNADDTLN LYFDEEEIFS ESRTLLQSYW AETSYQIQSL RDNPECAQQE FEQIQDREDP
     GLHVALSYDV NEDVAAPYIA SGQKPMVAIL REQGVNGQVE MAAAFDRAGF TAVDLHMSDI
     LSGRISLEQF QGLVACGGFS YGDVLGAGEG WAKSVLFNSR ARDQFAAFFE RESTFALGVC
     NGCQMMSNLH ELIPGAEHWP HFVRNESEQF EARVAMVEVQ SSPSVFLQGM AGSRMPIAIA
     HGEGRAEFAD SAHLQRLQQS GDVALRYVDN RGVVTERYPA NPNGSPAGIA GVTTPDGRVT
     IMMPHPERMF RAVQHSWKPD DWSEDGSWMR MFRNARAWLK
//
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