(data stored in SCRATCH3701 zone)

SWISSPROT: D5E9A2_METMS

ID   D5E9A2_METMS            Unreviewed;       332 AA.
AC   D5E9A2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 61.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|HAMAP-Rule:MF_00741};
DE            EC=6.3.3.1 {ECO:0000256|HAMAP-Rule:MF_00741};
DE   AltName: Full=AIR synthase {ECO:0000256|HAMAP-Rule:MF_00741};
DE   AltName: Full=AIRS {ECO:0000256|HAMAP-Rule:MF_00741};
DE   AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|HAMAP-Rule:MF_00741};
GN   Name=purM {ECO:0000256|HAMAP-Rule:MF_00741};
GN   OrderedLocusNames=Mmah_0220 {ECO:0000313|EMBL:ADE35753.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35753.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35753.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + ATP = 5-
CC         amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58478, ChEBI:CHEBI:137981,
CC         ChEBI:CHEBI:456216; EC=6.3.3.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00741};
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00741}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741}.
CC   -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00741}.
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DR   EMBL; CP001994; ADE35753.1; -; Genomic_DNA.
DR   RefSeq; WP_013036696.1; NC_014002.1.
DR   EnsemblBacteria; ADE35753; ADE35753; Mmah_0220.
DR   GeneID; 8982352; -.
DR   KEGG; mmh:Mmah_0220; -.
DR   eggNOG; arCOG00639; Archaea.
DR   eggNOG; COG0150; LUCA.
DR   HOGENOM; HOG000229091; -.
DR   KO; K01933; -.
DR   OMA; EPLFMTD; -.
DR   OrthoDB; 62508at2157; -.
DR   BioCyc; MMAH547558:G1GHT-218-MONOMER; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02196; PurM; 1.
DR   Gene3D; 3.30.1330.10; -; 1.
DR   Gene3D; 3.90.650.10; -; 1.
DR   HAMAP; MF_00741; AIRS; 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   PANTHER; PTHR10520; PTHR10520; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   SUPFAM; SSF55326; SSF55326; 1.
DR   SUPFAM; SSF56042; SSF56042; 1.
DR   TIGRFAMs; TIGR00878; purM; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9A2.
DR   SWISS-2DPAGE; D5E9A2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00741};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00741, ECO:0000313|EMBL:ADE35753.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00741};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          53..158
FT                   /note="AIRS"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          171..323
FT                   /note="AIRS_C"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   332 AA;  36259 MW;  E60CEF8D89EC2B6C CRC64;
     MDKKLTYADS GVDIHQEEST IGNLTGDMTY TREGLGAPMT SIGHYAGLMD FGDFALAMAT
     DGVGSKVLIA NEMEKWDTMG IDCIAMNVND LIAIGAEPIS FVDYLAIEKH SDEFARQIGV
     GLAKGAEISR MSILGGETAT LPEIVKGFDL AGTCLGKVDK DAIITGEKVA EGDVLVGVPS
     SGVHSNGYTL VRKIIENSKY SYHDPLPYDS SRTIGEELLT PTRIYMEVLD TIRKCEVHGL
     AHITGSGLLK LRRVSELGFD ITDPIEPPEI FRFLQKEGNV EELEMYRTFN MGMGFLLIVP
     PHEAQKVAEI VDGKIVGRIT EKDIRVKDLI IE
//

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