(data stored in ACNUC7421 zone)

SWISSPROT: C7QJA1_CATAD

ID   C7QJA1_CATAD            Unreviewed;       228 AA.
AC   C7QJA1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 52.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurQ {ECO:0000256|HAMAP-Rule:MF_00421};
DE            Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00421};
DE            EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00421};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit I {ECO:0000256|HAMAP-Rule:MF_00421};
DE            Short=FGAR amidotransferase I {ECO:0000256|HAMAP-Rule:MF_00421};
DE            Short=FGAR-AT I {ECO:0000256|HAMAP-Rule:MF_00421};
DE   AltName: Full=Glutaminase PurQ {ECO:0000256|HAMAP-Rule:MF_00421};
DE            EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00421};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000256|HAMAP-Rule:MF_00421};
GN   Name=purQ {ECO:0000256|HAMAP-Rule:MF_00421};
GN   OrderedLocusNames=Caci_0290 {ECO:0000313|EMBL:ACU69243.1};
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:ACU69243.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69243.1, 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_00421, ECO:0000256|SAAS:SAAS00371060}.
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_00421, ECO:0000256|SAAS:SAAS00371035}.
CC   -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3).
CC       {ECO:0000256|HAMAP-Rule:MF_00421, ECO:0000256|SAAS:SAAS00064583}.
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_00421, ECO:0000256|SAAS:SAAS00371024}.
CC   -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1
CC       PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_00421,
CC       ECO:0000256|SAAS:SAAS00371066}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421,
CC       ECO:0000256|SAAS:SAAS00371042}.
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DR   EMBL; CP001700; ACU69243.1; -; Genomic_DNA.
DR   RefSeq; WP_012784538.1; NC_013131.1.
DR   ProteinModelPortal; C7QJA1; -.
DR   STRING; 479433.Caci_0290; -.
DR   EnsemblBacteria; ACU69243; ACU69243; Caci_0290.
DR   KEGG; cai:Caci_0290; -.
DR   eggNOG; ENOG4105D21; Bacteria.
DR   eggNOG; COG0047; LUCA.
DR   HOGENOM; HOG000238240; -.
DR   KO; K01952; -.
DR   OMA; NCDRDVA; -.
DR   OrthoDB; POG091H0A3G; -.
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-KW.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
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   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00421; PurQ; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ.
DR   PIRSF; PIRSF001586; FGAM_synth_I; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01737; FGAM_synth_I; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QJA1.
DR   SWISS-2DPAGE; C7QJA1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00064591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00064586};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00064582};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00448455};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00064592, ECO:0000313|EMBL:ACU69243.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00064590};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00064605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN        4    228       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   ACT_SITE     87     87       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00421}.
FT   ACT_SITE    195    195       {ECO:0000256|HAMAP-Rule:MF_00421}.
FT   ACT_SITE    197    197       {ECO:0000256|HAMAP-Rule:MF_00421}.
SQ   SEQUENCE   228 AA;  24264 MW;  B6B05977D9940722 CRC64;
     MPARIGVVTF PGTLDDRQAL RAAAAVGAEP VALWHKDRDL HQVDAVVLPG GFSYGDYLRA
     GAIARFSPVM DTIIDAARDG LPVLGICNGF QVLCETHLLE GAMIRNGDLH FINRDVTLRI
     ENNRTAWTSD YEDGAEAVIP IKNVDGRFVA DEPTLDALEA EGRVLARYVA NPNGAARDIA
     GITNAAGNVV GLMPHPEYAI DDLTGPHPGP GTDGLPFFTS ILKSLVSA
//

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