(data stored in ACNUC7421 zone)

SWISSPROT: C7QJA8_CATAD

ID   C7QJA8_CATAD            Unreviewed;       361 AA.
AC   C7QJA8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 68.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|HAMAP-Rule:MF_00741, ECO:0000256|SAAS:SAAS00812269};
DE            EC=6.3.3.1 {ECO:0000256|HAMAP-Rule:MF_00741, ECO:0000256|SAAS:SAAS00812272};
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=Caci_0297 {ECO:0000313|EMBL:ACU69250.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69250.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69250.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + 2-(formamido)-N(1)-(5-phospho-D-
CC       ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole. {ECO:0000256|HAMAP-Rule:MF_00741,
CC       ECO:0000256|SAAS:SAAS00768662}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-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, ECO:0000256|SAAS:SAAS00768623}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741,
CC       ECO:0000256|SAAS:SAAS00812270}.
CC   -!- SIMILARITY: Belongs to the AIR synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00741, ECO:0000256|SAAS:SAAS00812279}.
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DR   EMBL; CP001700; ACU69250.1; -; Genomic_DNA.
DR   ProteinModelPortal; C7QJA8; -.
DR   STRING; 479433.Caci_0297; -.
DR   EnsemblBacteria; ACU69250; ACU69250; Caci_0297.
DR   KEGG; cai:Caci_0297; -.
DR   eggNOG; ENOG4105CXB; Bacteria.
DR   eggNOG; COG0150; LUCA.
DR   HOGENOM; HOG000229090; -.
DR   KO; K01933; -.
DR   OMA; NHCVNDI; -.
DR   OrthoDB; POG091H0128; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000000851; 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-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP.
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; AIR_synth_C_dom.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR004733; PurM_cligase.
DR   PANTHER; PTHR10520:SF42; PTHR10520:SF42; 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; C7QJA8.
DR   SWISS-2DPAGE; C7QJA8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00741,
KW   ECO:0000256|SAAS:SAAS00768570};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741,
KW   ECO:0000256|SAAS:SAAS00812276};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00741,
KW   ECO:0000256|SAAS:SAAS00768591, ECO:0000313|EMBL:ACU69250.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00741,
KW   ECO:0000256|SAAS:SAAS00768645};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00741,
KW   ECO:0000256|SAAS:SAAS00812278};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN       59    163       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      175    340       AIRS_C. {ECO:0000259|Pfam:PF02769}.
SQ   SEQUENCE   361 AA;  36781 MW;  1FAE110B6C793295 CRC64;
     MSGATYAAAG VDIEAGDRAV ELMKEWVAKT RRPEVLGGIG GFAGLFDASA LKAYDRPLLA
     TSTDGVGTKV AIAQRMDRHD TIGRDLVGMV VDDLVVCGAE PLFMTDYIAT GKVVPEVIAG
     IVKGIAEGCV LAGCALVGGE TAEHPGLLKP GEYDVAGAGT GVVEADKVLG AERVREGDVL
     VAMASSGAHS NGYSLLRHVF FDVAGWELDR DVPEFGRTLG EELLEPTRIY SLDCLALIEA
     AEVHAISHIT GGGVAANIAR IIPAGLEARL DRGTWTPPAV FGTVGALGGV ATLELEKTLN
     MGVGMVAVLP AASVDPALAL LNARGLPSWV CGEVVASEGA VTVGGAKGGD GAASLHGDYA
     G
//

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