ID F4KLT0_PORAD Unreviewed; 1233 AA.
AC F4KLT0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:AEE13165.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:AEE13165.1};
GN OrderedLocusNames=Poras_1225 {ECO:0000313|EMBL:AEE13165.1};
OS Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 /
OS JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides asaccharolyticus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE13165.1, ECO:0000313|Proteomes:UP000006545};
RN [1] {ECO:0000313|Proteomes:UP000006545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC {ECO:0000313|Proteomes:UP000006545};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002689; AEE13165.1; -; Genomic_DNA.
DR RefSeq; WP_013760586.1; NC_015501.1.
DR AlphaFoldDB; F4KLT0; -.
DR STRING; 879243.Poras_1225; -.
DR MEROPS; C56.972; -.
DR KEGG; pah:Poras_1225; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_10; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000006545; Chromosome.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01740; GATase1_FGAR_AT; 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 InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
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 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEE13165.1};
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:UP000006545}.
FT DOMAIN 10..83
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 121..170
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 382..533
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 782..901
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1079
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1233 AA; 134240 MW; 87BF64A88982C074 CRC64;
MISYFVLGDT IYAVSHTSAL SEETCERLSW LFGGAQLAPE SQLEGTFVGP RPTQVTPWST
NAVEITQNMR ISGIDRIEQL TRTHEAKPHY DPMLQAIYKG LGQESFAMTA EPQPIREITD
LAAYNEEEGL ALSEEEIAYL QSVSARIGRP LTDSEVFGFS QVNSEHCRHK IFNGTFVIDG
LRQNDSLFAM IKQTSKENPN GIVSAYKDNV AFVKGPRVWQ FAPTSATEPS LFTLRERNTV
LALKAETHNF PTTVEPFNGA ATGSGGEIRD RMCGGKGSLP LSGSAVYITS YPRLEKDQKL
SPAKLDPRPW LYQSPQEILT KASDGASDFG NKFGQPLING SLLTFEHQEG ADSTLYGYDK
VIMLAGGMGY APQEDAKKET PQPGETVVLL GGDNYRIGMG GGAVSSVATG EYSSGIELNA
VQRANPEMQK RVLNVVRAIS EQGDNPIVSI HDHGAGGHLN CLTELIEETG GRIDIDALPV
GDPTLSAREI IGNESQERVG LLIQEREYAQ MEQIARREGS PIYKVGETTD DERLLFSTER
EGRAAIDLAV SDLLGQSPKT VMEDETVAHK FAPVSYDKEL WREYLDKVLT LEAVASKDWL
TNKVDRSVTG RVAQQQCVGA LQLPLSDLGA MALDYDGKSG MATAVGHAPQ VALIDAGAGS
RMAIAEALTN IVFAPIEGGI RGISLSANWM WPCRNKGEDA RLYEAVQACS EFAIDLGINI
PTGKDSLSMT QKYPDGKQVM SPGTLIITAA APVSDVRGIV TPELKAAKQS RLLYIDFSFA
PMALGGSALA QALGQLGDSF PTVGDTDYFA TAFEAVQELI HKGLVLAGHD ISAGGMVTTL
LEMCFANTHG GAEICLDELS NVDLVTALYS ENPGIILQVS KAEQAKRILE EYEIAYADLG
APTESRLLMI HKESKTYEID IDAARKCWAN KSYLLDCFQS GEAPATSRYE NLGKQPVQWR
FPHAFAGTYA GLGLEPHRTK ASGIKAAILR DNGTNGEREM AYALHLAGFD VEDIHLTDLI
EGRTDLADVR MLVYCGGFSH SDVLGSAKGW AAGILYNERA RKAIEAFYAR PDTLSLGICN
GCQLMAQLGL LGKDAQGKSL FKLEHNASHK FESNFLTVDI ADTGAILTQG LEGCQLGVWV
AHGEGRFVCP TIPDEQIAAR YHYDTYPGNP NGSERSIAAL CSSDGRHLAM MPHPERATLT
WQCGFYPEER RQEDQVSPWI QFFRNGYEWL AKQ
//
