(data stored in ACNUC1104 zone)

SWISSPROT: D5USA1_TSUPD

ID   D5USA1_TSUPD            Unreviewed;       590 AA.
AC   D5USA1;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01643};
DE   AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
DE   AltName: Full=Formate-dependent GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01643};
DE            EC=2.1.2.- {ECO:0000256|HAMAP-Rule:MF_01643};
DE   AltName: Full=GAR transformylase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
DE            Short=GART 2 {ECO:0000256|HAMAP-Rule:MF_01643};
DE   AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000256|HAMAP-Rule:MF_01643};
DE   AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
GN   Name=purT {ECO:0000256|HAMAP-Rule:MF_01643};
GN   OrderedLocusNames=Tpau_0527 {ECO:0000313|EMBL:ADG77168.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS   NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77168.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG77168.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA   Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain
RT   (no. 33).";
RL   Stand. Genomic Sci. 4:342-351(2011).
CC   -!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes
CC       the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR),
CC       producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is
CC       provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
CC       {ECO:0000256|HAMAP-Rule:MF_01643, ECO:0000256|SAAS:SAAS01090368}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + formate + N(1)-(5-phospho-D-ribosyl)glycinamide =
CC         ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide +
CC         phosphate; Xref=Rhea:RHEA:24829, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58426, ChEBI:CHEBI:58457, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01643,
CC         ECO:0000256|SAAS:SAAS01124177};
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:0000256|HAMAP-Rule:MF_01643, ECO:0000256|SAAS:SAAS00083138}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01643,
CC       ECO:0000256|SAAS:SAAS01092012}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP-
CC       Rule:MF_01643, ECO:0000256|SAAS:SAAS01092022}.
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DR   EMBL; CP001966; ADG77168.1; -; Genomic_DNA.
DR   RefSeq; WP_013125210.1; NC_014158.1.
DR   STRING; 521096.Tpau_0527; -.
DR   EnsemblBacteria; ADG77168; ADG77168; Tpau_0527.
DR   KEGG; tpr:Tpau_0527; -.
DR   eggNOG; ENOG4107SPG; Bacteria.
DR   eggNOG; COG0027; LUCA.
DR   HOGENOM; HOG000072820; -.
DR   OMA; GMVTMIT; -.
DR   OrthoDB; 1677960at2; -.
DR   BioCyc; TPAU521096:G1GKO-510-MONOMER; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000001213; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 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; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005862; PurT.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF01370; Epimerase; 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;
DR   PRODOM; D5USA1.
DR   SWISS-2DPAGE; D5USA1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01643, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|SAAS:SAAS00098858};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001213};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01643,
KW   ECO:0000256|SAAS:SAAS01090363};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01643,
KW   ECO:0000256|SAAS:SAAS00249036};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01643,
KW   ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00467005};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01643,
KW   ECO:0000256|SAAS:SAAS00467012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01643,
KW   ECO:0000256|SAAS:SAAS00083129, ECO:0000313|EMBL:ADG77168.1}.
FT   DOMAIN      133    333       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   NP_BIND     174    179       ATP. {ECO:0000256|HAMAP-Rule:MF_01643}.
FT   NP_BIND     209    212       ATP. {ECO:0000256|HAMAP-Rule:MF_01643}.
FT   REGION       35     36       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01643}.
FT   REGION      387    388       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01643}.
FT   METAL       292    292       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01643}.
FT   METAL       304    304       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01643}.
FT   BINDING      95     95       5'-phosphoribosylglycinamide.
FT                                {ECO:0000256|HAMAP-Rule:MF_01643}.
FT   BINDING     128    128       ATP. {ECO:0000256|HAMAP-Rule:MF_01643}.
FT   BINDING     169    169       ATP. {ECO:0000256|HAMAP-Rule:MF_01643}.
FT   BINDING     217    217       ATP. {ECO:0000256|HAMAP-Rule:MF_01643}.
FT   BINDING     311    311       5'-phosphoribosylglycinamide.
FT                                {ECO:0000256|HAMAP-Rule:MF_01643}.
FT   BINDING     380    380       5'-phosphoribosylglycinamide.
FT                                {ECO:0000256|HAMAP-Rule:MF_01643}.
SQ   SEQUENCE   590 AA;  62196 MW;  BDA3DCC6C05B200E CRC64;
     MMDPMTNLTE TGGNPRIGTA LTPGATKVLL LGSGELGKEV LIAFQRLGVE TIAVDRYANA
     PAMQVAHRSH VVDMTDADAV RRVIEQEKPR YVVPEIEALA TEALIAVEEE GVAEVIPTAR
     AVSLTMDREG IRKLAAEDLG LPCSPYAFAS SVEELRTGAR EVGFPCVVKP VMSSSGKGQT
     VVRTPDEIDG AWEAAVTGGR VRNERVIVEG FVDFDYEITL LTVRVFDSER GKVITRFCEP
     IGHRQQGGDY VESWQPQPMS QTAYDSATSV AGRITTALGD GGTGGRGVFG VELFVKGDDV
     YFSEVSPRPH DTGLVTLGSQ RLSEFELHAR AILGMPVDSS LMSPAASAVI YGTKDSSSVA
     FDNVARALDI PETDIRLFGK PEGYAKRRLG VVVATADTVE VARANAQEAA NRVQVVDSSD
     PVDPGAPATV AVPIQRPQVQ EDMSTRAIPT QRPAPQAPPS PPAHPGPAAP PPASAPPTSA
     SPVVRPKQAP PAAPPTAASP VVRPGAGRVA PPAPQAPRSG DGAADVPSGP TAMHPVATRR
     PAQPRPIQPQ RRPAVSSPTA PEADSQQVAE EYDHNPPTSM GMAPQRPHQD
//

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