ID Q5AUA9_EMENI Unreviewed; 1360 AA.
AC Q5AUA9; C8V6N2;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 24-JAN-2024, entry version 112.
DE RecName: Full=phosphoribosylformylglycinamidine synthase {ECO:0000256|ARBA:ARBA00012747};
DE EC=6.3.5.3 {ECO:0000256|ARBA:ARBA00012747};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|ARBA:ARBA00032632};
DE AltName: Full=Formylglycinamide ribotide amidotransferase {ECO:0000256|ARBA:ARBA00029823};
GN ORFNames=ANIA_08121 {ECO:0000313|EMBL:CBF73928.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF73928.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004920}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000256|ARBA:ARBA00008608}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BN001302; CBF73928.1; -; Genomic_DNA.
DR RefSeq; XP_681390.1; XM_676298.1.
DR STRING; 227321.Q5AUA9; -.
DR MEROPS; C56.972; -.
DR EnsemblFungi; CBF73928; CBF73928; ANIA_08121.
DR GeneID; 2869027; -.
DR KEGG; ani:AN8121.2; -.
DR VEuPathDB; FungiDB:AN8121; -.
DR eggNOG; KOG1907; Eukaryota.
DR HOGENOM; CLU_001031_0_2_1; -.
DR InParanoid; Q5AUA9; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000560; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR NCBIfam; TIGR01735; FGAM_synt; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR SUPFAM; SSF82697; PurS-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560}.
FT DOMAIN 38..158
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 182..234
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 448..601
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 864..1013
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1191
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1322
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1360 AA; 147384 MW; 08BFC39309606DDA CRC64;
MASPFDSADF ALPGSIAYSR SRGRAIAASI GAQDVRGQWV HYVHTAERLP EFQQDVLQQL
LSYGDITDIP PSFTAEDGEF DVFYVFPRTG TISPWSSQAT GIAHVCGLRK YVKRIERGIK
ISCLRPASGE YKPGFKDVLH DRMTQLISET EPDLHLMFSE HSPLPLETIP LSGSDKSPKE
VLQEANKRMG LALEESEIEY LAAAYGPDGP LARDPTDVEL FMFAQVNSEH CRHKQFNASW
TIDGMEMPNS LFSMIRNTHR KNPEFTVSAY SDNAAVLQGF DSSFWAPDSV TGEWNHTKEI
VHFLAKVETH NHPTAVSPYP GAATGSGGEI RDEGAVGRGS KPKAGLAGYC VSDLLIPGLK
QPWELDIGKP NHIASALDIM LEAPIGSAAF NNEFGRPCIT GYFRTLLTEI DIGDGEKEVR
GYHKPIMIAG GVGTVRPQHA IKKPDAVKPG SYLVVLGGPA MLIGLGGGAA SSITSGEGSV
DLDFASVQRG NAEVQRRAQE VINACTAMGD NNPIKFIHDV GAGGLSNALP ELIHDSGLGA
KFELREIDSA DRSMSPMQIW CCEAQERYVM AVGEEGMNKF TAICHRERCG FSVVGRGEGG
SEEEKRLILL DRESKEHPTV IDLPLSVLFG KPPRMTRTVD SRKLKLPAVD TSLTTYLPSL
APNRAELIGE AANRVLSLPA VGSKSFLITI GDRTVGGLTA RDQMVGRWQT PVSDVAVTAT
ALVQGAKTGE AMAMGEKPTL ALISPGASAR MAVAESLMNI AAADLVDRLS RVKLSANWKA
ASSHPGEGAA IYEAVEAIGM HLCPELGISI PVGKDSMSMK MKWKDESGAK EVTAPMSLVI
SAFAPVENFR KTWTPALRHP EDVGDTVLMF VDLSLGRKAM GGSALAQVFN QVGSECPDIR
NVELFKDFFD ATQQLQEAGI VLAYHDRSDG GLFTTLAEMM FAGRCGVEIL LDNICPNLDT
SSFIETLFNE ELGAVFQVRK EHEMQFRSCF ATCGPPAGLI HKIGRVSERP KQNLAIYYKA
SQVYRNTRAN LQQTWASTSY HMQRIRDNAA CADQEYANIL DDTDPGLSWN PTFDPKDRAL
PFLTSLTSMS PFANKPRVAI LREQGVNSQA EMAFAFNTAG FAAIDVHMTD IISGRVSLSS
FVGLAACGGF SYGDVLGAGQ GWAKSVLLHD NTRAEFQSFF NRPDTFALGV CNGCQFLSRL
SSLIPGASNW PTFERNASEQ YEGRVAMVRI SDPDPSNPSV FLHGMHGSSF PIAVAHGEGR
ASFTASSTDP ASFVAQGLAP VQWVDNATLK PTMKYPFNPN GSPEGIAGIR NANGRVMAIM
PHPERTVMNG IASWLPAKAE EWGDIGPWGR IFFSARRWVG
//
