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Formate-dependent phosphoribosylglycinamide formyltransferase (5'-phosphoribosylglycinamide transformylase 2) (Formate-dependent GAR transformylase) (EC 2.1.2.-) (GAR transformylase 2) (GART 2) (Non-folate glycinamide ribonucleotide transformylase) (Phosphoribosylglycinamide formyltransferase 2)

 F0S354_DESTD            Unreviewed;       393 AA.
F0S354;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
03-MAY-2011, sequence version 1.
27-SEP-2017, entry version 48.
RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01643};
AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
AltName: Full=Formate-dependent GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01643};
EC=2.1.2.- {ECO:0000256|HAMAP-Rule:MF_01643};
AltName: Full=GAR transformylase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
Short=GART 2 {ECO:0000256|HAMAP-Rule:MF_01643};
AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000256|HAMAP-Rule:MF_01643};
AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
Name=purT {ECO:0000256|HAMAP-Rule:MF_01643};
OrderedLocusNames=Dester_0625 {ECO:0000313|EMBL:ADY73276.1};
Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae;
Desulfurobacterium.
NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY73276.1, ECO:0000313|Proteomes:UP000007102};
[1] {ECO:0000313|Proteomes:UP000007102}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
US DOE Joint Genome Institute (JGI-PGF);
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
Brambilla E., Klenk H.-P., Eisen J.A.;
"The complete genome of Desulfurobacterium thermolithotrophum DSM
11699.";
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes
the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR),
producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is
provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
{ECO:0000256|HAMAP-Rule:MF_01643, ECO:0000256|SAAS:SAAS00701003}.
-!- CATALYTIC ACTIVITY: Formate + ATP + 5'-phospho-ribosylglycinamide
= 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate.
{ECO:0000256|HAMAP-Rule:MF_01643}.
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-
phospho-D-ribosyl)glycinamide (formate route): step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01643, ECO:0000256|SAAS:SAAS00650280}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01643,
ECO:0000256|SAAS:SAAS00703122}.
-!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP-
Rule:MF_01643, ECO:0000256|SAAS:SAAS00653163}.
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EMBL; CP002543; ADY73276.1; -; Genomic_DNA.
RefSeq; WP_013638233.1; NC_015185.1.
STRING; 868864.Dester_0625; -.
EnsemblBacteria; ADY73276; ADY73276; Dester_0625.
KEGG; dte:Dester_0625; -.
eggNOG; ENOG4108HH9; Bacteria.
eggNOG; COG0027; LUCA.
KO; K08289; -.
OMA; GMVTMIT; -.
OrthoDB; POG091H03TI; -.
UniPathway; UPA00074; UER00127.
Proteomes; UP000007102; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:UniProtKB-UniRule.
GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 3.30.1490.20; -; 1.
HAMAP; MF_01643; PurT; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR003135; ATP-grasp_carboxylate-amine.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR016185; PreATP-grasp_dom.
InterPro; IPR005862; PurT.
Pfam; PF02222; ATP-grasp; 1.
SUPFAM; SSF52440; SSF52440; 1.
TIGRFAMs; TIGR01142; purT; 1.
PROSITE; PS50975; ATP_GRASP; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01643, ECO:0000256|PROSITE-
ProRule:PRU00409, ECO:0000256|SAAS:SAAS00653136};
Complete proteome {ECO:0000313|Proteomes:UP000007102};
Lyase {ECO:0000313|EMBL:ADY73276.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01643,
ECO:0000256|SAAS:SAAS00701002};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01643,
ECO:0000256|SAAS:SAAS00650272};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01643,
ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00653136};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01643,
ECO:0000256|SAAS:SAAS00653155};
Reference proteome {ECO:0000313|Proteomes:UP000007102};
Transferase {ECO:0000256|HAMAP-Rule:MF_01643,
ECO:0000256|SAAS:SAAS00650268, ECO:0000313|EMBL:ADY73276.1}.
DOMAIN 118 308 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
NP_BIND 159 164 ATP. {ECO:0000256|HAMAP-Rule:MF_01643}.
NP_BIND 194 197 ATP. {ECO:0000256|HAMAP-Rule:MF_01643}.
REGION 21 22 5'-phosphoribosylglycinamide binding.
{ECO:0000256|HAMAP-Rule:MF_01643}.
REGION 362 363 5'-phosphoribosylglycinamide binding.
{ECO:0000256|HAMAP-Rule:MF_01643}.
METAL 267 267 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01643}.
METAL 279 279 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01643}.
BINDING 81 81 5'-phosphoribosylglycinamide.
{ECO:0000256|HAMAP-Rule:MF_01643}.
BINDING 113 113 ATP. {ECO:0000256|HAMAP-Rule:MF_01643}.
BINDING 154 154 ATP. {ECO:0000256|HAMAP-Rule:MF_01643}.
BINDING 202 202 ATP. {ECO:0000256|HAMAP-Rule:MF_01643}.
BINDING 286 286 5'-phosphoribosylglycinamide.
{ECO:0000256|HAMAP-Rule:MF_01643}.
BINDING 355 355 5'-phosphoribosylglycinamide.
{ECO:0000256|HAMAP-Rule:MF_01643}.
SEQUENCE 393 AA; 43834 MW; CF8D1C9C54726699 CRC64;
MKIGTPLSHN STQVLLLGSG ELGKEFALEA LRLGIEVIAV DNYQFAPAQQ VAQRFYVIDM
KDGSQIKNIV YREKPDFIVP EIEAIDTDVL LELEEEGFNV VPCAKAVKYT MDRIGIRRLA
AEELGLKTSK YRFASDLESY KKAVKEIGLP VVVKPVMSSS GKGQSIVRKE EEIDEAFFYA
QRNARGKGNA VIIEEFIDFD FEITLLTVRT KEQGTLFCEP IGHVQVDGDY QESWQPQPMT
ETALKRAKEM AKAITDALGG YGIFGCEFFV KEDEVWFSEV SPRPHDTGMV TMITQNMSEF
EIHLRAILGL PMDIKLISPG ASHCFHAKGF GVAPRYEGIE KALSIPDTTV KIFGKPTTRP
RRRMGITLAT ADTVDEARKK AKEAALKIKV IES


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