ID M1YW45_NITG3 Unreviewed; 367 AA.
AC M1YW45;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00020367};
DE EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047};
DE AltName: Full=AIR synthase {ECO:0000256|ARBA:ARBA00032931};
DE AltName: Full=AIRS {ECO:0000256|ARBA:ARBA00033093};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|ARBA:ARBA00031908};
GN Name=purM {ECO:0000313|EMBL:CCQ89534.1};
GN ORFNames=NITGR_110014 {ECO:0000313|EMBL:CCQ89534.1};
OS Nitrospina gracilis (strain 3/211).
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Nitrospina.
OX NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ89534.1, ECO:0000313|Proteomes:UP000011704};
RN [1] {ECO:0000313|EMBL:CCQ89534.1, ECO:0000313|Proteomes:UP000011704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3/211 {ECO:0000313|EMBL:CCQ89534.1,
RC ECO:0000313|Proteomes:UP000011704};
RX PubMed=23439773; DOI=10.3389/fmicb.2013.00027;
RA Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.;
RT "The genome of Nitrospina gracilis illuminates the metabolism and evolution
RT of the major marine nitrite oxidizer.";
RL Front. Microbiol. 4:27-27(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023392};
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 2/2.
CC {ECO:0000256|ARBA:ARBA00004686}.
CC -!- SIMILARITY: Belongs to the AIR synthase family.
CC {ECO:0000256|ARBA:ARBA00010280}.
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:CCQ89534.1}.
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DR EMBL; CAQJ01000013; CCQ89534.1; -; Genomic_DNA.
DR RefSeq; WP_005006074.1; NZ_HG422173.1.
DR AlphaFoldDB; M1YW45; -.
DR STRING; 1266370.NITGR_110014; -.
DR HOGENOM; CLU_047116_0_0_0; -.
DR InParanoid; M1YW45; -.
DR OrthoDB; 9802507at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000011704; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02196; PurM; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004733; PurM_cligase.
DR NCBIfam; TIGR00878; purM; 1.
DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCQ89534.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011704}.
FT DOMAIN 52..161
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 178..345
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 367 AA; 39619 MW; C7BD1F278F0EA17B CRC64;
MPNNNPTPSK YEESGVSQTG AETALDHILK HILPTRQFNT EFPVKADIGY FANVIDLGNG
TGVALCTDGV GTKMRVAEMM HQYDTIGIDC VAMNVNDLIC IGAKPVSMVD YIACSHLEPQ
VFDQLGQGLA EGARQAGISI SGGEISQIRE IICGIDLIGA ALGHIQLDRI NTGQNIAEGN
LILGIASSGV HSNGLTLARR VLLGETEDEQ KENVHKYEES LERTLGAELL EPTYIYVPAV
LEMFDTGLDL RALVHITGGG LLNLLRVQKK GIRFVIDPLP DIPPVFSLIQ QRGEISDAEM
YEVFNMGVGF CVIVEHANDA EAVQKICKRH GISCHGIGYV ETTGDDGKEV VIPSKKLKSE
GGHFTPM
//
