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Database: UniProt/TrEMBL
Entry: A8EVB3_ARCB4
LinkDB: A8EVB3_ARCB4
Original site: A8EVB3_ARCB4 
ID   A8EVB3_ARCB4            Unreviewed;       737 AA.
AC   A8EVB3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   26-NOV-2014, entry version 59.
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   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   ECO:0000313|EMBL:ABV67886.1};
GN   OrderedLocusNames=Abu_1639 {ECO:0000313|EMBL:ABV67886.1};
OS   Arcobacter butzleri (strain RM4018).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Arcobacter.
OX   NCBI_TaxID=367737 {ECO:0000313|EMBL:ABV67886.1, ECO:0000313|Proteomes:UP000001136};
RN   [1] {ECO:0000313|EMBL:ABV67886.1, ECO:0000313|Proteomes:UP000001136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM4018 {ECO:0000313|EMBL:ABV67886.1,
RC   ECO:0000313|Proteomes:UP000001136};
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G.,
RA   Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the
RT   Epsilonproteobacterium Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(2007).
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}.
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DR   EMBL; CP000361; ABV67886.1; -; Genomic_DNA.
DR   RefSeq; YP_001490556.1; NC_009850.1.
DR   ProteinModelPortal; A8EVB3; -.
DR   STRING; 367737.Abu_1639; -.
DR   EnsemblBacteria; ABV67886; ABV67886; Abu_1639.
DR   GeneID; 5623498; -.
DR   KEGG; abu:Abu_1639; -.
DR   PATRIC; 20964640; VBIArcBut20197_1611.
DR   eggNOG; COG0046; -.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; QAVVFKI; -.
DR   OrthoDB; EOG6FNHHR; -.
DR   BioCyc; ABUT367737:GHWO-1637-MONOMER; -.
DR   UniPathway; UPA00074; UER00128.
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   HAMAP; MF_00420; PurL_2; 1.
DR   InterPro; IPR010918; AIR_synth_C_dom.
DR   InterPro; IPR000728; AIR_synth_N_dom.
DR   InterPro; IPR010074; PRibForGlyAmidine_synth_II.
DR   InterPro; IPR016188; PurM_N-like.
DR   Pfam; PF00586; AIRS; 2.
DR   Pfam; PF02769; AIRS_C; 2.
DR   SUPFAM; SSF55326; SSF55326; 2.
DR   SUPFAM; SSF56042; SSF56042; 2.
DR   TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001136};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00420, ECO:0000313|EMBL:ABV67886.1};
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:UP000001136}.
FT   REGION       93     96       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00420}.
FT   REGION      316    318       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE     48     48       {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   ACT_SITE     94     94       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL        92     92       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       116    116       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       272    272       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       536    536       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING      51     51       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING      90     90       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     115    115       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     244    244       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     498    498       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     535    535       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     538    538       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
SQ   SEQUENCE   737 AA;  79761 MW;  36D88E431F0585B9 CRC64;
     MQKKEMNIQE IALAHSLTLE EFENIKEILG REPNYVEIGI FSAMWSEHCS YKSSKKYLSG
     FPTKAPWVIQ GPGENAGVID IGDGYAAVFK MESHNHPSFI EPYQGAATGV GGILRDVFTM
     GARPIANMNS IRFASIEGDS ETAQKHRYLL KGVVAGIGGY GNCMGVPTIG GETTFEECYA
     GNNLVNAFTL GLAKADEIFY GKAEGIGNPV MYVGSKTGRD GLGGAVMSSA AFDEDSESKR
     PTVQVGDPFT EKLLLEACLE LFKADLIVGI QDMGAAGLTS SSFEMAGRSG SGMIMHLDKV
     PAREEGMTPY DFMLSESQER MLICAKKGCE QAIIDIFQKW ELDVAVIGEV TATGNMELFW
     HGEKVAEVPV QPVSEQAPIL DRPVKKPAYL DGIENISLDK ELSNQVVFDE LFSDMEVVDK
     SWVYSQYDSM VQTNTIKGPG SLDGSSIRIK ETGKALSMSA DCNTRFCYIN PELGAAAAVM
     ESGRNVAMTG AVPKAITDCL NFGNPTNPEV MWQFKECCEG IKKACKDLNT PVIGGNVSLY
     NETNGVGVFP TPSIAMVGVN DDANKVLPSK LQENGNILYL LGETKSEFGG SLYLKKLYGK
     VAGVHPEVSF EKELALWNTV IEANKLGLLK AAKDVNVGGI AIALAKMAVV GNKGIEVNIS
     LNDSKDIFSE SLSRAIVEVN PSNCEAFEKI AKSFGLECTK IGVVKGNKIS INDIYKDLDK
     VSDVYFNRFK QVIEQVS
//
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