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Database: UniProt
Entry: Q8NM23
LinkDB: Q8NM23
Original site: Q8NM23 
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   26-NOV-2014, entry version 84.
DE   RecName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE            Short=GART 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE            EC=2.1.2.- {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=Formate-dependent GAR transformylase {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=GAR transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
GN   Name=purT {ECO:0000255|HAMAP-Rule:MF_01643};
GN   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. {ECO:0000255|HAMAP-
CC       Rule:MF_01643}.
CC   -!- CATALYTIC ACTIVITY: Formate + ATP + 5'-phospho-ribosylglycinamide
CC       = 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01643}.
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       {ECO:0000255|HAMAP-Rule:MF_01643}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01643}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC       Rule:MF_01643}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01643}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC00153.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAF20781.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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   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; cgl:NCgl2663; -.
DR   PATRIC; 21497556; VBICorGlu203724_2690.
DR   eggNOG; COG0027; -.
DR   HOGENOM; HOG000072820; -.
DR   KO; K08289; -.
DR   OMA; AWEYAMS; -.
DR   OrthoDB; EOG6GJBVD; -.
DR   UniPathway; UPA00074; UER00127.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:UniProtKB-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   Pfam; PF02222; ATP-grasp; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   NP_BIND     164    169       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   NP_BIND     199    202       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION       25     26       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION      372    373       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   METAL       277    277       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   METAL       289    289       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   BINDING      85     85       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     118    118       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     159    159       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     207    207       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     277    277       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     289    289       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     296    296       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     365    365       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
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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