(data stored in ACNUC7421 zone)

SWISSPROT: C7QJA2_CATAD

ID   C7QJA2_CATAD            Unreviewed;       787 AA.
AC   C7QJA2;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE            Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00420};
DE            EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00420};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
DE            Short=FGAR amidotransferase II {ECO:0000256|HAMAP-Rule:MF_00420};
DE            Short=FGAR-AT II {ECO:0000256|HAMAP-Rule:MF_00420};
DE   AltName: Full=Glutamine amidotransferase PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
GN   Name=purL {ECO:0000256|HAMAP-Rule:MF_00420};
GN   OrderedLocusNames=Caci_0291 {ECO:0000313|EMBL:ACU69244.1};
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:ACU69244.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69244.1, 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_00420}.
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_00420}.
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_00420}.
CC   -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1
CC       PurL, 1 PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_00420}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420}.
CC   -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00420}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00420}.
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DR   EMBL; CP001700; ACU69244.1; -; Genomic_DNA.
DR   RefSeq; WP_012784539.1; NC_013131.1.
DR   ProteinModelPortal; C7QJA2; -.
DR   STRING; 479433.Caci_0291; -.
DR   EnsemblBacteria; ACU69244; ACU69244; Caci_0291.
DR   KEGG; cai:Caci_0291; -.
DR   eggNOG; ENOG4107QIK; Bacteria.
DR   eggNOG; COG0046; LUCA.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; FIEPYQG; -.
DR   OrthoDB; POG091H009J; -.
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:0000287; F:magnesium ion 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; 3.30.1330.10; -; 2.
DR   Gene3D; 3.90.650.10; -; 2.
DR   HAMAP; MF_00420; PurL_2; 1.
DR   InterPro; IPR010918; AIR_synth_C_dom.
DR   InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
DR   InterPro; IPR016188; PurM-like_N.
DR   PANTHER; PTHR43555; PTHR43555; 1.
DR   Pfam; PF00586; AIRS; 2.
DR   Pfam; PF02769; AIRS_C; 2.
DR   PIRSF; PIRSF001587; FGAM_synthase_II; 1.
DR   SUPFAM; SSF55326; SSF55326; 2.
DR   SUPFAM; SSF56042; SSF56042; 2.
DR   TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QJA2.
DR   SWISS-2DPAGE; C7QJA2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00420, ECO:0000313|EMBL:ACU69244.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN      117    219       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      232    385       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   DOMAIN      484    598       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      611    753       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   REGION      124    127       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00420}.
FT   REGION      343    345       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE     76     76       {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   ACT_SITE    125    125       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       123    123       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       147    147       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       299    299       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       574    574       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING      79     79       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     121    121       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     146    146       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     271    271       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     536    536       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     573    573       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     576    576       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
SQ   SEQUENCE   787 AA;  83395 MW;  B172596EFDDE4121 CRC64;
     MSNGNSSENV FDTTDVFVDT AVSFDTVAKA AQTPDVKQPF RELGMTEDEY LRVREILGRR
     PSSSELAMYS VMWSEHCSYK SSRVHLKQFG EKAPKTAALL VGPGENAGVV DVGEGLAVTF
     KVESHNHPSY VEPYQGAATG VGGIVRDILT MGARPIAVMD PLRFGPADAP DTARVLPGVV
     AGVGGYGNCL GVPNIGGEIV FDPCYLGNPL VNALCVGVMR ADEIKLAKAP GPGNQVILFG
     ARTGGDGIGG ASVLASATFD EDGPAKRPSV QVGDPFMEKV LIECCLEIFA ADLVVGIQDL
     GAAGLTCSTT ELAAAGTGGM DVRLDLAPLR DSTLTPEEVL MSESQERMMA VVEPAKVEAF
     LAVCDKWDVT ATALGEVTDT GRLRMWWHGE IIVDVPPRTL AHEGPVYNRP FARPEWQDAL
     QADAPTAERL KRPGNAEELR ETLLRLVGSP NLADKTWAVE QYDHRVQGNT VLGHGEDSGM
     VRLDAALPGT SLGVALSTDG NGRFAKLDPY QGAQLALAEA YRNVAATGAK PLAVTDCLNF
     GSPEDPDVMW QFAEACRGLA DACLELGTPV TGGNVSFYNQ TGELNIHPTP VVGVLGVIDD
     VDRRTRSAFE REGEILLLLG DTRDEFGGSE WAHEVHGHLG GLPPRLDLQR EKVLGEVLIA
     GSRDGMLSAA HDLSDGGLAQ AVVEGCLRGG HGARLVLPET DADGAALDPF VALFAESAGR
     ALVAVPRSEE LRFTDMCVAR GLPVARVGVV DGDVLEVQGQ FTVPMAELRT AHEAPFRKLF
     GHSVVDA
//

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