(data stored in ACNUC7421 zone)

SWISSPROT: A0LFD0_SYNFM

ID   A0LFD0_SYNFM            Unreviewed;      1009 AA.
AC   A0LFD0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE            Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00420};
DE            EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00420};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
DE            Short=FGAR amidotransferase II {ECO:0000256|HAMAP-Rule:MF_00420};
DE            Short=FGAR-AT II {ECO:0000256|HAMAP-Rule:MF_00420};
DE   AltName: Full=Glutamine amidotransferase PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
GN   Name=purL {ECO:0000256|HAMAP-Rule:MF_00420};
GN   OrderedLocusNames=Sfum_0432 {ECO:0000313|EMBL:ABK16132.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16132.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16132.1, 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: Part of the phosphoribosylformylglycinamidine synthase
CC       complex involved in the purines biosynthetic pathway. Catalyzes
CC       the ATP-dependent conversion of formylglycinamide ribonucleotide
CC       (FGAR) and glutamine to yield formylglycinamidine ribonucleotide
CC       (FGAM) and glutamate. The FGAM synthase complex is composed of
CC       three subunits. PurQ produces an ammonia molecule by converting
CC       glutamine to glutamate. PurL transfers the ammonia molecule to
CC       FGAR to form FGAM in an ATP-dependent manner. PurS interacts with
CC       PurQ and PurL and is thought to assist in the transfer of the
CC       ammonia molecule from PurQ to PurL. {ECO:0000256|HAMAP-
CC       Rule:MF_00420}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-D-
CC         ribosyl)glycinamide = 2-(formamido)-N(1)-(5-phospho-D-
CC         ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58426, ChEBI:CHEBI:58478,
CC         ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00420, ECO:0000256|SAAS:SAAS01143401};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000256|HAMAP-
CC       Rule:MF_00420, ECO:0000256|SAAS:SAAS01143431}.
CC   -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1
CC       PurL, 1 PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_00420}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420}.
CC   -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00420}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00420}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000478; ABK16132.1; -; Genomic_DNA.
DR   RefSeq; WP_011697305.1; NC_008554.1.
DR   STRING; 335543.Sfum_0432; -.
DR   EnsemblBacteria; ABK16132; ABK16132; Sfum_0432.
DR   KEGG; sfu:Sfum_0432; -.
DR   eggNOG; ENOG4107QIK; Bacteria.
DR   eggNOG; COG0046; LUCA.
DR   HOGENOM; HOG000238228; -.
DR   KO; K01952; -.
DR   OMA; FIEPYQG; -.
DR   OrthoDB; 26038at2; -.
DR   BioCyc; SFUM335543:G1G7I-440-MONOMER; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1330.10; -; 2.
DR   Gene3D; 3.90.650.10; -; 2.
DR   HAMAP; MF_00420; PurL_2; 1.
DR   InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
DR   InterPro; IPR041609; PurL_linker.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   PANTHER; PTHR43555; PTHR43555; 1.
DR   Pfam; PF00586; AIRS; 2.
DR   Pfam; PF02769; AIRS_C; 2.
DR   Pfam; PF18072; FGAR-AT_linker; 1.
DR   SUPFAM; SSF55326; SSF55326; 2.
DR   SUPFAM; SSF56042; SSF56042; 2.
PE   3: Inferred from homology;
DR   PRODOM; A0LFD0.
DR   SWISS-2DPAGE; A0LFD0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143413};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143366, ECO:0000313|EMBL:ABK16132.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143383};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143388};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143406};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143445};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT   DOMAIN      190    248       FGAR-AT_linker. {ECO:0000259|Pfam:
FT                                PF18072}.
FT   DOMAIN      296    419       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      435    585       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   DOMAIN      677    785       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      828    976       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   REGION      542    544       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE    245    245       {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   ACT_SITE    316    316       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       314    314       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       338    338       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       499    499       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     337    337       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     471    471       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     735    735       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     780    780       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     783    783       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
SQ   SEQUENCE   1009 AA;  110495 MW;  161B0F686CDC55A8 CRC64;
     MATRLEISLK EHLFDAEGAG LCRKIKDYFG WDVQRARVIH ILTLDTGLTG VELEAVRKEI
     FTNPVTQVSV YGTSAVRFDW AIWVGYRPGV RDTAGSVAVE AISDLLGRKL GAEESAYTSR
     LYLLSGTRLG KTEVETVARE LLANDIVQQW RIYRYDEWDP AGGVGIILPR VVLPHTPETR
     EMPIESPEDL MRLSDERNLA LNPLDVPVIL DYFARPEVVR ARREMGLGAP TDVELEAISQ
     ARSDHCNHNT FRGKFHYRDL ATGERTVVDN LFKTCIEAPT LAIQAEKDWV VSVLWDNAGV
     ARFDDNNNYV ITGETHNSPS NMEAYGGALT GIVGIYRDIM GTGKGARLTA GLYGYCVGPK
     DYRGPLRPHL HPRRLLDGIV EGVKDGGNKH GVPTPFGNLF FHPSFLGKCL VFVAALGIMP
     RLVRGEPSDL KRPDPGDFII MSGGRVGKDG IHGVTASSEI YSESTPAGHV QIGDPYTQKK
     MHDFLLEARD EGLISFITDN GGGGLSSSVG ESARFCGGAR VELDKVPLKY EGLDQWEIWV
     SESQERMTVA VNPRHLDRFM ELSRRHEVES TAIGTYGSDG RLHLTYRGKT CACLDLSLFT
     EAFPQWEFEA DWQPPDNRGL HEPVLAEPAD YGRLLHDVLA RPNVCSREWI QRQYDHEVQG
     GSVIKLMTGV DRDVPNDAAV LRPALESRRG LAVSQSINPT YSAIDTYHMV AATIDEAVRR
     LVAVGGRLEE IGGVDNFCWP SVQYDPVSNP DGRYKAAQLV RANWALRDIC LAFGIPLLSG
     KDSMYVDGHL GGAYGERHKI SGLPTMQFTA TTVVPDISDC QTMDVKTAGD LVYVLGWTHD
     ELGGSEYYDC FGYLGRNVPE LDPESVLPVY RVVEKAIREG LVASCHGIYR GGLGVHAAMA
     AMAGGLGMRL DLEKVPVAHA GAQAKSGPGP RDDHILFSES CGRFILTVSP AMRGAFEAMA
     GGLPCAPVGE VLAEPVFVVA GRSGNVLLEE PVGELKHSWK FGAGGERGE
//

If you have problems or comments...

PBIL Back to PBIL home page