(data stored in ACNUC7421 zone)

SWISSPROT: A0LFD2_SYNFM

ID   A0LFD2_SYNFM            Unreviewed;       283 AA.
AC   A0LFD2;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01930};
DE            EC=2.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01930};
DE   AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|HAMAP-Rule:MF_01930};
DE   AltName: Full=GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01930};
DE            Short=GART {ECO:0000256|HAMAP-Rule:MF_01930};
GN   Name=purN {ECO:0000256|HAMAP-Rule:MF_01930};
GN   OrderedLocusNames=Sfum_0434 {ECO:0000313|EMBL:ABK16134.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16134.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16134.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a formyl group from 10-
CC       formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR),
CC       producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and
CC       tetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01930}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-D-
CC         ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) +
CC         N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide;
CC         Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57454, ChEBI:CHEBI:58426, ChEBI:CHEBI:58457;
CC         EC=2.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01930};
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 (10-formyl THF route): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01930}.
CC   -!- SIMILARITY: Belongs to the GART family. {ECO:0000256|HAMAP-
CC       Rule:MF_01930}.
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DR   EMBL; CP000478; ABK16134.1; -; Genomic_DNA.
DR   RefSeq; WP_011697307.1; NC_008554.1.
DR   STRING; 335543.Sfum_0434; -.
DR   EnsemblBacteria; ABK16134; ABK16134; Sfum_0434.
DR   KEGG; sfu:Sfum_0434; -.
DR   eggNOG; ENOG4108V3E; Bacteria.
DR   eggNOG; COG0299; LUCA.
DR   HOGENOM; HOG000033575; -.
DR   OrthoDB; 1815747at2; -.
DR   BioCyc; SFUM335543:G1G7I-442-MONOMER; -.
DR   UniPathway; UPA00074; UER00126.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd08645; FMT_core_GART; 1.
DR   HAMAP; MF_01930; PurN; 1.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR004607; GART.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   TIGRFAMs; TIGR00639; PurN; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LFD2.
DR   SWISS-2DPAGE; A0LFD2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01930};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01930,
KW   ECO:0000313|EMBL:ABK16134.1}.
FT   DOMAIN        9    230       Formyl_trans_N. {ECO:0000259|Pfam:
FT                                PF00551}.
FT   REGION       18     20       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01930}.
FT   REGION      134    137       10-formyltetrahydrofolate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01930}.
FT   ACT_SITE    157    157       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01930}.
FT   BINDING      99     99       10-formyltetrahydrofolate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01930}.
FT   BINDING     155    155       10-formyltetrahydrofolate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01930}.
FT   SITE        193    193       Raises pKa of active site His.
FT                                {ECO:0000256|HAMAP-Rule:MF_01930}.
SQ   SEQUENCE   283 AA;  31687 MW;  DB3968C96446F111 CRC64;
     MSESDSRLRI AVLVSGSGTN LQALIDRARD GRLAAEIVVV ASDRPGIRGL ARAEAAGIPA
     RVVDYRGFLK QDWTVLERKL PVDVDAVDRA QNILHHEDRE ERLKRLVRLM SAEAEMIAAI
     EAYRPDYVCL AGFMRLVTPF FLHHFNRAGK LRVINIHPAL LPAFPGQHGY EDTFSYGCRW
     GGITIHFVDE GEDSGPIIAQ AVYPILPEDD VEKVRQRGLQ LEYEMYAQVI NWLAAGRVEL
     VPAAGGRART VIRDPEYSRI MESWVRKVLD AGPQDCRFSD PSA
//

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