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Multifunctional fusion protein [Includes: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (GARS) (Glycinamide ribonucleotide synthetase) (Phosphoribosylglycinamide synthetase); N5-carboxyaminoimidazole ribonucleotide mutase (N5-CAIR mutase) (EC 5.4.99.18) (5-(carboxyamino)imidazole ribonucleotide mutase)]

 E1QDM8_DESB2            Unreviewed;       589 AA.
E1QDM8;
30-NOV-2010, integrated into UniProtKB/TrEMBL.
30-NOV-2010, sequence version 1.
18-JUL-2018, entry version 62.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000256|HAMAP-Rule:MF_01929};
Includes:
RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138};
EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138};
AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
Includes:
RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929};
EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929};
AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
Name=purE {ECO:0000256|HAMAP-Rule:MF_01929};
Synonyms=purD {ECO:0000256|HAMAP-Rule:MF_00138};
OrderedLocusNames=Deba_0168 {ECO:0000313|EMBL:ADK83547.1};
Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / VKM B-1802 /
2st14).
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales;
Desulfarculaceae; Desulfarculus.
NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK83547.1, ECO:0000313|Proteomes:UP000009047};
[1] {ECO:0000313|EMBL:ADK83547.1, ECO:0000313|Proteomes:UP000009047}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
{ECO:0000313|Proteomes:UP000009047};
PubMed=21304732;
Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G.,
Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
Jeffries C.D., Detter J.C., Han C., Rohde M., Brambilla E., Goker M.,
Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
Kyrpides N.C., Klenk H.P., Land M.;
"Complete genome sequence of Desulfarculus baarsii type strain
(2st14).";
Stand. Genomic Sci. 3:276-284(2010).
-!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole
ribonucleotide (CAIR). {ECO:0000256|HAMAP-Rule:MF_01929}.
-!- CATALYTIC ACTIVITY: 5-carboxyamino-1-(5-phospho-D-
ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
carboxylate. {ECO:0000256|HAMAP-Rule:MF_01929}.
-!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP
+ phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
{ECO:0000256|HAMAP-Rule:MF_00138}.
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
{ECO:0000256|HAMAP-Rule:MF_01929}.
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
ribose 1-diphosphate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00138}.
-!- SIMILARITY: Belongs to the AIR carboxylase family. Class I
subfamily. {ECO:0000256|HAMAP-Rule:MF_01929}.
-!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP-
Rule:MF_00138}.
-----------------------------------------------------------------------
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EMBL; CP002085; ADK83547.1; -; Genomic_DNA.
RefSeq; WP_013257003.1; NC_014365.1.
ProteinModelPortal; E1QDM8; -.
STRING; 644282.Deba_0168; -.
EnsemblBacteria; ADK83547; ADK83547; Deba_0168.
KEGG; dbr:Deba_0168; -.
eggNOG; ENOG4105C12; Bacteria.
eggNOG; COG0041; LUCA.
eggNOG; COG0151; LUCA.
HOGENOM; HOG000033463; -.
KO; K01945; -.
OMA; KATVCKY; -.
OrthoDB; POG091H02DZ; -.
BioCyc; DBAA644282:G1GM5-166-MONOMER; -.
UniPathway; UPA00074; UER00125.
UniPathway; UPA00074; UER00943.
Proteomes; UP000009047; Chromosome.
GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:InterPro.
GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
Gene3D; 3.30.1490.20; -; 1.
Gene3D; 3.40.50.7700; -; 1.
Gene3D; 3.90.600.10; -; 1.
HAMAP; MF_00138; GARS; 1.
HAMAP; MF_01929; PurE_classI; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
InterPro; IPR000115; PRibGlycinamide_synth.
InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
InterPro; IPR020559; PRibGlycinamide_synth_CS.
InterPro; IPR020562; PRibGlycinamide_synth_N.
InterPro; IPR033747; PurE_ClassI.
InterPro; IPR000031; PurE_dom.
InterPro; IPR035893; PurE_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
Pfam; PF00731; AIRC; 1.
Pfam; PF01071; GARS_A; 1.
Pfam; PF02843; GARS_C; 1.
Pfam; PF02844; GARS_N; 1.
SMART; SM01001; AIRC; 1.
SMART; SM01210; GARS_C; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52255; SSF52255; 1.
SUPFAM; SSF52440; SSF52440; 1.
TIGRFAMs; TIGR00877; purD; 1.
TIGRFAMs; TIGR01162; purE; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS00184; GARS; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000009047};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01929};
Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:ADK83547.1};
Lyase {ECO:0000313|EMBL:ADK83547.1};
Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
Reference proteome {ECO:0000313|Proteomes:UP000009047}.
DOMAIN 107 314 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
COILED 566 586 {ECO:0000256|SAM:Coils}.
BINDING 437 437 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01929}.
BINDING 440 440 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01929}.
BINDING 467 467 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01929}.
SEQUENCE 589 AA; 60741 MW; 6C21647540B8649F CRC64;
MKILVIGGGG REHAIVWKLA QSPKVQAIFC APGNPGMAGL ATCLTIDPDD IAGLKAFALD
NHIDLTVVGP EAPLVAGLTD VFEQAGLLVA GPSAAAARLE GSKAFAKEVM EAAGVPTAQC
RIFDDAAQAK DHCRNLGGPV VVKADGLAAG KGVIMCRTAG EAMAACERIM EERAFGQAGE
RVVIEEWLEG EEASFLVFTD GQAIAAMPSS QDHKAVGEGD TGPNTGGMGA YSPAPVVGPA
LESAVIERVI KPTLAEMKRR GAPFKGVLYA GLMIDKAGEP KVLEFNVRFG DPECQPLLMR
LDSDLAEILQ LLAQGRLAEA EVEWKADPAV CVVLASGGYP GDYAKGFEIS GVEEANAVEG
ARVFHAGTAL KDGKLVNAGG RVLGVCATGV DIAQAIERAY EACGKIWWQG MLLRRDIGHR
ALARLKNRPL VGIVMGSPND WEVMKSAAKA LTELGVPHEA RVLSAHRTPG QAAQYAASAA
ERGLKVIIAG AGWAAHLAGA MAAQTVLPVI GVPIGSSQLN GLDALLSTVQ MPPGIPVATV
AIGAGGARNA GVLAAQILAL GDAALAQGLA QQRRDMAAEV AAAEKKLFA


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