(data stored in ACNUC7421 zone)

SWISSPROT: C7QJA0_CATAD

ID   C7QJA0_CATAD            Unreviewed;        88 AA.
AC   C7QJA0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurS {ECO:0000256|HAMAP-Rule:MF_01926};
DE            Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_01926};
DE            EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_01926};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit III {ECO:0000256|HAMAP-Rule:MF_01926};
DE            Short=FGAR amidotransferase III {ECO:0000256|HAMAP-Rule:MF_01926};
DE            Short=FGAR-AT III {ECO:0000256|HAMAP-Rule:MF_01926};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit III {ECO:0000256|HAMAP-Rule:MF_01926};
GN   Name=purS {ECO:0000256|HAMAP-Rule:MF_01926};
GN   OrderedLocusNames=Caci_0289 {ECO:0000313|EMBL:ACU69242.1};
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:ACU69242.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69242.1, 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   -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC       complex involved in the purines biosynthetic pathway. Catalyzes
CC       the ATP-dependent conversion of formylglycinamide ribonucleotide
CC       (FGAR) and glutamine to yield formylglycinamidine ribonucleotide
CC       (FGAM) and glutamate. The FGAM synthase complex is composed of
CC       three subunits. PurQ produces an ammonia molecule by converting
CC       glutamine to glutamate. PurL transfers the ammonia molecule to
CC       FGAR to form FGAM in an ATP-dependent manner. PurS interacts with
CC       PurQ and PurL and is thought to assist in the transfer of the
CC       ammonia molecule from PurQ to PurL. {ECO:0000256|HAMAP-
CC       Rule:MF_01926}.
CC   -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D-
CC       ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-
CC       (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_01926}.
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 1/2. {ECO:0000256|HAMAP-
CC       Rule:MF_01926}.
CC   -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1
CC       PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_01926}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01926}.
CC   -!- SIMILARITY: Belongs to the PurS family. {ECO:0000256|HAMAP-
CC       Rule:MF_01926}.
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DR   EMBL; CP001700; ACU69242.1; -; Genomic_DNA.
DR   ProteinModelPortal; C7QJA0; -.
DR   STRING; 479433.Caci_0289; -.
DR   EnsemblBacteria; ACU69242; ACU69242; Caci_0289.
DR   KEGG; cai:Caci_0289; -.
DR   eggNOG; ENOG410839H; Bacteria.
DR   eggNOG; COG1828; LUCA.
DR   HOGENOM; HOG000033801; -.
DR   KO; K01952; -.
DR   OMA; VIENYRF; -.
DR   OrthoDB; POG091H0894; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.1280.10; -; 1.
DR   HAMAP; MF_01926; PurS; 1.
DR   InterPro; IPR003850; PurS.
DR   PANTHER; PTHR34696; PTHR34696; 1.
DR   Pfam; PF02700; PurS; 1.
DR   ProDom; PD010362; FGAM_PurS; 1.
DR   TIGRFAMs; TIGR00302; TIGR00302; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QJA0.
DR   SWISS-2DPAGE; C7QJA0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
SQ   SEQUENCE   88 AA;  9653 MW;  71B4FD8976AF7203 CRC64;
     MARVLVDVML KPEILDPQGQ AVQRALPRMG FDSVTNVRQG KRFELELADA DPATLRATAE
     QMAEKLLANT VIEDFKVTVL PADSSENA
//

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