ID D1AW67_STRM9 Unreviewed; 1236 AA.
AC D1AW67;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:ACZ00543.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:ACZ00543.1};
GN OrderedLocusNames=Smon_0046 {ECO:0000313|EMBL:ACZ00543.1};
OS Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 /
OS 9901).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Streptobacillus.
OX NCBI_TaxID=519441 {ECO:0000313|EMBL:ACZ00543.1, ECO:0000313|Proteomes:UP000002072};
RN [1] {ECO:0000313|EMBL:ACZ00543.1, ECO:0000313|Proteomes:UP000002072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14647 / DSM 12112 / NCTC 10651 / 9901
RC {ECO:0000313|Proteomes:UP000002072};
RX PubMed=21304670; DOI=10.4056/sigs.48727;
RA Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S.,
RA Del Rio T.G., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D.,
RA Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C.,
RA Ovchinikova G., Pati A., Mavromatis K., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Sproer C., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Streptobacillus moniliformis type strain
RT (9901T).";
RL Stand. Genomic Sci. 1:300-307(2009).
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DR EMBL; CP001779; ACZ00543.1; -; Genomic_DNA.
DR RefSeq; WP_012858101.1; NC_013515.1.
DR AlphaFoldDB; D1AW67; -.
DR STRING; 519441.Smon_0046; -.
DR GeneID; 29672828; -.
DR KEGG; smf:Smon_0046; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_003100_2_0_0; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000002072; Chromosome.
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; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 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; IPR010141; FGAM_synthase.
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 NCBIfam; TIGR01857; FGAM-synthase; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000313|EMBL:ACZ00543.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000002072}.
FT DOMAIN 174..222
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 438..589
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1077
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1236 AA; 139060 MW; E927378D00DDAD82 CRC64;
MSDLRFFVEK KKHCNFERRR LLKQLQEELG VVSLKDIRIL NCYDIFGCPN DMEDIKKMIL
SEPVTDDIFE KLELNDEKYF AIEYLPGQFD QRAHSAMQCI DILISNKNVE ITTSKIFIIY
GEVSNDELQK IKNYIINPIE TREKNLNILK KEKINVNTNI IQYNNFINLN SDELENLRKN
LGLSMTYEDI LHIQNYYKSE KRNPTETEIK VFDTYWSDHC RHSTFETKIN NVKFPDSEYG
KFLNLEFKKY LEIKEIVSKH KNITLMDMAT VVAKYFKKIG KLDNLEISEE NNACSIYIDV
ETEKFNGEKN IEKWLLMFKN ETHNHPTEIE PFGGAATCLG GAIRDPLSGR AYVYQAIRVT
GSANPLESIE NTLKGKLSQK KITTGAAHGY SSYGNQIGIA TSLVSEIYHE GYKAKRMEVG
AVVAAAPLEN VVRKTPENGD SIILLGGKTG RDGCGGATGS SKEHTNKSIF LCGSEVQKGN
APEERKIQRL FRNGNVTKLI KKCNDFGAGG VAVAIGELAD GIDVNLDLIP VKYEGLSGTE
LAISESQERM AVVVAKEYVE EFLKEAEKEN LLATVVGKIT DNERLILRYR GKEIVNISRG
FLNTNGATQE IDIKIENIDV KDFLSRDLSS NTFKEKWLEN IEKLNVASTK GLSEMFDSSI
GASTVLMPYG GKYQLSPIDV SIMKIPMISK KTNTSSAITW GYNPYLTEKS PYHGSMYAVL
ESIAKLVASG TSYDGIYLSF QEYFEKLGKD NVKWSKPMLA LLGAMRCQLD FEIAAIGGKD
SMSGTFENIS VPPTLISFAV NTVNAKDVIS TEIKEVGNRI YLVENKINDD LSYNSKDIKE
KYSKVLDEIK KGKILSAKVV GMGGIAGTLS QMCFGNKIGI KLDNLDLDYF KYMPGSIIVE
SKEELDFTLI GESIKEFNIT FKDEVIDLEK LLYLWLNKLD NVFPYEYKEE KKEYINISKP
KIIDYSSSIK VAKPRVLITA FPGTNCEYDM KNIFERNGAI TNITLFKNLN RTHIESSIDE
ICKELKNSQI FVIPGGFSAG DEPDGSGKFI ATVLQNPKIK EEIERFLQRD GLILGICNGF
QALVKSGLLP YGNIGEITED SPTLTYNKIG RHISQMVKTR ISTNRSPWLS SFNVGDEFDL
PVSHGEGRFF ASEKTLQKLI ENGQVATQYV DFNGKATNEF KFNPNGSEFA IEGIISPDGK
IFGKMGHSER TGENILKNVS GNKYQNIFKN GIEYFK
//
