ID C0ZKC6_BREBN Unreviewed; 747 AA.
AC C0ZKC6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 29-MAY-2013, entry version 34.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase 2;
DE EC=6.3.5.3;
DE AltName: Full=Phosphoribosylformylglycinamidine synthase II;
GN Name=purL; OrderedLocusNames=BBR47_06000;
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC Brevibacillus.
OX NCBI_TaxID=358681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599;
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H.,
RA Yoshikawa H., Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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.
CC -!- SUBUNIT: Heterodimer of two subunits, PurQ and PurL (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the FGAMS family.
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DR EMBL; AP008955; BAH41577.1; -; Genomic_DNA.
DR RefSeq; YP_002770081.1; NC_012491.1.
DR ProteinModelPortal; C0ZKC6; -.
DR STRING; 358681.BBR47_06000; -.
DR EnsemblBacteria; BAH41577; BAH41577; BBR47_06000.
DR GeneID; 7716339; -.
DR KEGG; bbe:BBR47_06000; -.
DR PATRIC; 21231484; VBIBreBre96763_0596.
DR eggNOG; COG0046; -.
DR HOGENOM; HOG000238227; -.
DR KO; K01952; -.
DR OMA; WSEHCCY; -.
DR ProtClustDB; CLSK2547083; -.
DR BioCyc; BBRE358681:GHYS-693-MONOMER; -.
DR UniPathway; UPA00074; UER00128.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:HAMAP.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.650.10; -; 1.
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; SSF56042; AIR_synth_C; 2.
DR SUPFAM; SSF55326; PurM_N-like; 2.
DR TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Purine biosynthesis.
FT NP_BIND 113 124 ATP (By similarity).
SQ SEQUENCE 747 AA; 79210 MW; 1A17E9530EE07E53 CRC64;
MSQLTHKEPT AEQIADQKLY KEIGLTDEEY QRVVEILGRK PNWTETGLYS VMWSEHCSYK
NSKPVLRRFP TKGPRVLQGP GEGAGIVDIG DNQAVVFKIE SHNHPSAIEP YQGAATGVGG
IIRDVFSMGA RPIALLNSLR FGELKSPRVK YLFENVVAGI AGYGNCIGIP TVGGEVNFDP
TYEGNPLVNA MCVGLIDHEK IQKGVASGIG NPVIYVGAST GRDGIHGATF ASEELTEESE
KKRPAVQVGD PFMEKLLLEA CLELIDTGIV VGIQDMGAAG LTSSSSEMAS KAGNGIEMNL
DLVPQREAGM SAYEMMLSES QERMLVVVEK GKEAEAIAIF DKWGLASAVV GKVTEDSKLR
LLHQGEVVAE VPVDSLANDA PVYHRPSAVP AYYEANANVD VLAAIQEPKD LNGTLKSLLA
QPTVANKAWV YEQYDHIVRA NTAVKPGSDA AVVMVRGTRK ALAMSTDCNG RYVYLDPKVG
GAIAVAESAR NVVCSGAEPL AITDCLNFGS PEKPEVFWQF EKSCEGMSEA CVALDAPVIG
GNVSFYNERS GDAIYPTPTV GMVGLITDVD HITTQDFKNE GDAIILLGET FAELGGSEYQ
KMATGSISGR PPQIDLTKEA AVQKLVLTAI RQGLVNSAHD LSEGGLGVAL AESCFGKGVG
AQVTLTSEMR IDALLFSESQ SRILLSASGE QAAAILALAG ELGVPAENIG TVGGDHLVVN
VNGTEAINAS TQEVKAAWKD AIPCLIG
//
