ID PURT_CORGL Reviewed; 408 AA.
AC Q8NM23; Q6M293;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 01-MAY-2013, entry version 74.
DE RecName: Full=Phosphoribosylglycinamide formyltransferase 2;
DE Short=GART 2;
DE EC=2.1.2.-;
DE AltName: Full=5'-phosphoribosylglycinamide transformylase 2;
DE AltName: Full=Formate-dependent GAR transformylase;
DE AltName: Full=GAR transformylase 2;
GN Name=purT; OrderedLocusNames=Cgl2759, cg3054;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
OS LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT and its impact on the production of L-aspartate-derived amino acids
RT and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Catalyzes two reactions: the first one is the production
CC of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP
CC and beta GAR; the second, a side reaction, is the production of
CC acetyl phosphate and ADP from acetate and ATP (By similarity).
CC -!- CATALYTIC ACTIVITY: Formate + ATP + 5'-phospho-ribosylglycinamide
CC = 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-
CC phospho-D-ribosyl)glycinamide (formate route): step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the PurK/PurT family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC00153.1; Type=Erroneous initiation;
CC Sequence=CAF20781.1; Type=Erroneous initiation;
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DR EMBL; BA000036; BAC00153.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927156; CAF20781.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_601954.1; NC_003450.3.
DR RefSeq; YP_226997.1; NC_006958.1.
DR HSSP; P33221; 1KJ8.
DR ProteinModelPortal; Q8NM23; -.
DR SMR; Q8NM23; 7-401.
DR STRING; 196627.cg3054; -.
DR EnsemblBacteria; BAC00153; BAC00153; BAC00153.
DR EnsemblBacteria; CAF20781; CAF20781; cg3054.
DR GeneID; 1020704; -.
DR GeneID; 3344709; -.
DR KEGG; cgb:cg3054; -.
DR KEGG; cgl:NCgl2663; -.
DR PATRIC; 21497556; VBICorGlu203724_2690.
DR eggNOG; COG0027; -.
DR HOGENOM; HOG000072820; -.
DR KO; K08289; -.
DR OMA; HRQEKGD; -.
DR ProtClustDB; PRK09288; -.
DR BioCyc; CGLU196627:GJDM-2742-MONOMER; -.
DR UniPathway; UPA00074; UER00127.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:HAMAP.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR HAMAP; MF_01643; PurT; 1; -.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR InterPro; IPR005862; PurT.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR23047:SF2; PTHR23047:SF2; 1.
DR Pfam; PF02222; ATP-grasp; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 1.
DR TIGRFAMs; TIGR01142; purT; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1 408 Phosphoribosylglycinamide
FT formyltransferase 2.
FT /FTId=PRO_0000319152.
FT DOMAIN 123 318 ATP-grasp.
FT NP_BIND 164 169 ATP (By similarity).
FT NP_BIND 199 202 ATP (By similarity).
FT REGION 25 26 5'-phosphoribosylglycinamide binding (By
FT similarity).
FT REGION 372 373 5'-phosphoribosylglycinamide binding (By
FT similarity).
FT METAL 277 277 Magnesium (By similarity).
FT METAL 289 289 Magnesium (By similarity).
FT BINDING 85 85 5'-phosphoribosylglycinamide (By
FT similarity).
FT BINDING 118 118 ATP (By similarity).
FT BINDING 159 159 ATP (By similarity).
FT BINDING 207 207 ATP (By similarity).
FT BINDING 277 277 ATP (By similarity).
FT BINDING 289 289 ATP (By similarity).
FT BINDING 296 296 5'-phosphoribosylglycinamide (By
FT similarity).
FT BINDING 365 365 5'-phosphoribosylglycinamide (By
FT similarity).
SQ SEQUENCE 408 AA; 44050 MW; CE70F33C74AFA0D7 CRC64;
MYIPESIGTP LTPNATKVML LGSGELGKEV AIAFQRLGLE VHAVDRYEHA PAHQVAHFSY
VIDMTDAAQV RELVERVRPD FVIPEIEALA TDELVKIEEE GLATIVPTAR AAKLTMNREG
IRKLAAEELG LPTSNYEFCS TFEEFSAAAE KLGYPNVVKP VMSSSGKGQS VLRSSDDLQA
AWDYAMSGAR VANSRVIVEA FVEFDYEITL LTVRSIDPTT SKPATWFCEP IGHRQEDGDY
VESWQPMEMT PRALENARSV AARITNALGG RGVFGVELFV SGDDVYFSEV SPRPHDTGLV
TLATQRFSEF ELHAKAILGL PVDVTLISPG ASAVIYGGIE SEGVSYTGLA EALAVAETDL
RIFAKPEAFT KRRMGVAVST AEDVAAARDR ATLAAAAIKV HPGNSAEA
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