(data stored in ACNUC7421 zone)

SWISSPROT: B8ISZ7_METNO

ID   B8ISZ7_METNO            Unreviewed;       737 AA.
AC   B8ISZ7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
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=Mnod_0008 {ECO:0000313|EMBL:ACL55059.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55059.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55059.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001349; ACL55059.1; -; Genomic_DNA.
DR   RefSeq; WP_012634298.1; NC_011894.1.
DR   ProteinModelPortal; B8ISZ7; -.
DR   STRING; 460265.Mnod_0008; -.
DR   EnsemblBacteria; ACL55059; ACL55059; Mnod_0008.
DR   KEGG; mno:Mnod_0008; -.
DR   eggNOG; ENOG4108JIU; Bacteria.
DR   eggNOG; COG0046; LUCA.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; FIEPYQG; -.
DR   OrthoDB; POG091H009J; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000008207; 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; B8ISZ7.
DR   SWISS-2DPAGE; B8ISZ7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00420, ECO:0000313|EMBL:ACL55059.1};
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:UP000008207}.
FT   DOMAIN       87    188       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      202    351       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   DOMAIN      438    555       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      568    705       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   REGION       94     97       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00420}.
FT   REGION      312    314       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE     49     49       {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   ACT_SITE     95     95       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL        93     93       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       117    117       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       268    268       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       531    531       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING      52     52       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING      91     91       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     116    116       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     240    240       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     493    493       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     530    530       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     533    533       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
SQ   SEQUENCE   737 AA;  77929 MW;  FD1A20F42C16D4BD CRC64;
     MIRNDIAITP ELVRQHGLTE EEYARFKGLI GREPTITELG IVSAMWNEHC SYKSSRIHLR
     TLPTSAPWVI QGPGENAGVI DIGDGLACVF KMESHNHPSF IEPYQGAATG VGGILRDVFT
     MGARPIAALN ALRFGSPDHP RTRHLVAGVV AGIGGYGNSF GVPTVGGSVG FHRRYDGNIL
     VNAMAVGLAR ADAIFYAAAT GVGNPIVYLG SKTGRDGIHG ATMASAAFDE SSEEKRPTVQ
     VGDPFAEKLL LEACLELMAS GAVIAIQDMG AAGLTCSAVE MGAKGNLGVE LNLDAVPTRE
     PGMTAYEMML SESQERMLMV LKPGMEEQAK AIFVKWGLDF AIIGHTTDTL RFVIKHGGET
     VADLPIKELG DEAPVYDRPH RSNLYHPVLG PEEVPAPVTN VDALRRLVGS PDLASKRWVW
     EQYDHFILGN TVQKPGGDAA VVRVEDGPKG LALTTDVTPR YCEADPVEGG RQAVAEAYRN
     ISAVGGRPLA VTDNLNFGNP ERPEVMGQFV GCIHGIGEAC RALDFPVVSG NVSLYNETNG
     VGILPTPTIG GVGVVDDVRK TATIAFKREG DALVLIGRTE GWLGQSLYLA EICGREEGAP
     PPVDLAAERR NGEFVRGLIA SGLVDTVHDL SDGGLAVALA EMAMAGGIGA ALPECPLPVP
     CHAYLFGEDQ GRYLLAVDPE TLPDLLYSAS AQGIDAAVIG VTGADSLTLP GDETISVEEL
     RGVHEAWLPN YMAGPAA
//

If you have problems or comments...

PBIL Back to PBIL home page