ID A0A1E4T6M7_9ASCO Unreviewed; 1353 AA.
AC A0A1E4T6M7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=CANARDRAFT_26728 {ECO:0000313|EMBL:ODV87318.1};
OS [Candida] arabinofermentans NRRL YB-2248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX NCBI_TaxID=983967 {ECO:0000313|EMBL:ODV87318.1, ECO:0000313|Proteomes:UP000094801};
RN [1] {ECO:0000313|Proteomes:UP000094801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-2248 {ECO:0000313|Proteomes:UP000094801};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KV453848; ODV87318.1; -; Genomic_DNA.
DR STRING; 983967.A0A1E4T6M7; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000094801; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
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 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:UP000094801}.
FT DOMAIN 39..178
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 208..258
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 474..631
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 875..1001
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1181
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1313
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1353 AA; 147846 MW; 6081AED721D18641 CRC64;
MLITPGPQAL ASFRVANLIN DINKLVNSSV VLSVKSCQIH YIHYKNELDD DVLEKLKLLL
KYDDELDLSD ESNQLLYDLV QLSGDDSKSS EILSQKLDSD TYLIRVLPRP GTISPWSSKA
TNIVEVCGLG HQIDRVERGM AVLLKVREDF PIMQYFTSDN YASLSSIYDR MTQSVYISDN
IPKYNDLFED HEPKPLVYID VNSSADNLAK ANKELGLALD QGEMDYLLEA FRDTLGRNPT
DVELFMFAQV NSEHCRHKIF NADWKIDGEA KDMSLFQMIR NTHKLNPRYT ISAYSDNAAI
FQGPDAYHYA PDAKNGNKWT SKKEIVHTLI KVETHNHPTA VSPFPGAATG SGGEIRDEGA
VGRGSKSKCG LSGFSVSDLL IPDLRQPWEL DVGKPSHIAS PLDIMIEAPL GSAAFNNEFG
RPCISGYFRT LTTKVVNADK KQEIRGFHKP IMLAGGMGSV RPQLSLKSDL KITPGSAIIV
LGGQCMLIGL GGGAASSVSS GEGSADLDFA SVQRGNPEMQ RRAQEVINAC NAFGLDSPIQ
CIHDVGAGGL SNALPELVHD NDLGAKFELR DVLSLEPGMS PMEIWCNESQ ERYVLGVAQH
NLNQFKEICE RERCPYAVVG VATNEQRLVL TDRLLGSTPI DLDMSLLFGK PPKMSRQDVT
RPLLLEPVSI KPEVTIKDAL ARVLQLPSVG SKSFLITIAD RSVTGLIDRD QFVGPWQVPV
ADVGVTCTSF GDELVTTGEA LAMGEKPTLA LISPGASAKM CVAESLLNLY AADVKSLDSI
KLSANWMAPA TQPGEGAALY EAVQAIGLEL CPELDISIPV GKDSMSMKMS WDDKEVIAPM
SLVITAFSGV DDTSNTWTPM LQKSDDDTVL VLVDLAAKIS KSLGGSALAQ VYNQVGNSCP
TVHESAVLKG FLNAMSQLHK SSTVLAYHDR SDGGLIVTLL EMAFAGRCGL NIELNSLEDP
FTVLFNEELG GVFQIKKADY QSFVSILSSN GVSEKYVSVV GVPVFDLHHQ ITVSTNGTVV
VNQSRGELQQ TWSNTSYHMQ KLRDLPIAAD QEFQSILDNQ DPGLTYKLTF DPSDDLGLSS
LTTKPKVAIL REQGVNGQME MAWCFQQAGF EAHDVHMSDI ISGAVTLDDF VGLAACGGFS
YGDVLGAANG WATSVLYNDR ARSEFYKFFQ ERTDTFAFGA CNGCQFLSKI KSLIPGTENW
PSFERNKSQQ YEARVCTLEI IEENSETPLI FFDGMRGSRL PISVAHGEGL ASFGEGDKKL
DAFVDQGLVA AKFVDNYGVP TEKYPLNPNG SPNGIAGIRT PNGRVLAMMP HPERVVRLEA
NSYYPPELKD AWGGYGPWIR LFKNARKWVA ENN
//
