(data stored in SCRATCH zone)

SWISSPROT: D4YYH5_SPHJU

ID   D4YYH5_SPHJU            Unreviewed;       519 AA.
AC   D4YYH5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS00723629};
DE            EC=6.3.5.2 {ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS00723637};
DE   AltName: Full=GMP synthetase {ECO:0000256|HAMAP-Rule:MF_00344};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000256|HAMAP-Rule:MF_00344,
GN   ECO:0000313|EMBL:BAI95407.1};
GN   OrderedLocusNames=SJA_C1-05730 {ECO:0000313|EMBL:BAI95407.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95407.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95407.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC       {ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|SAAS:SAAS00723675}.
CC   -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP +
CC       diphosphate + GMP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00344,
CC       ECO:0000256|SAAS:SAAS00723670}.
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00344,
CC       ECO:0000256|SAAS:SAAS00723660}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00344,
CC       ECO:0000256|SAAS:SAAS00723681}.
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DR   EMBL; AP010803; BAI95407.1; -; Genomic_DNA.
DR   RefSeq; WP_013039131.1; NC_014006.1.
DR   ProteinModelPortal; D4YYH5; -.
DR   STRING; 452662.SJA_C1-05730; -.
DR   MEROPS; C26.A07; -.
DR   EnsemblBacteria; BAI95407; BAI95407; SJA_C1-05730.
DR   GeneID; 29272249; -.
DR   KEGG; sjp:SJA_C1-05730; -.
DR   eggNOG; ENOG4105CM0; Bacteria.
DR   eggNOG; COG0518; LUCA.
DR   eggNOG; COG0519; LUCA.
DR   HOGENOM; HOG000223965; -.
DR   KO; K01951; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; POG091H00MK; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00344; GMP_synthase; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR004739; GMP_synth_GATase.
DR   InterPro; IPR022955; GMP_synthase.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR   TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYH5.
DR   SWISS-2DPAGE; D4YYH5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00344, ECO:0000256|PROSITE-
KW   ProRule:PRU00886, ECO:0000256|SAAS:SAAS00723649};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00344,
KW   ECO:0000256|SAAS:SAAS00651347};
KW   GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_00344,
KW   ECO:0000256|PROSITE-ProRule:PRU00886, ECO:0000256|SAAS:SAAS00723668};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00344,
KW   ECO:0000256|SAAS:SAAS00723678, ECO:0000313|EMBL:BAI95407.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00344,
KW   ECO:0000256|PROSITE-ProRule:PRU00886, ECO:0000256|SAAS:SAAS00723622};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00344,
KW   ECO:0000256|PROSITE-ProRule:PRU00886, ECO:0000256|SAAS:SAAS00723677};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN        8    201       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   DOMAIN      202    394       GMPS ATP-PPase (ATP pyrophosphatase).
FT                                {ECO:0000259|PROSITE:PS51553}.
FT   NP_BIND     229    235       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00886}.
FT   ACT_SITE     85     85       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00344}.
FT   ACT_SITE    175    175       {ECO:0000256|HAMAP-Rule:MF_00344}.
FT   ACT_SITE    177    177       {ECO:0000256|HAMAP-Rule:MF_00344}.
SQ   SEQUENCE   519 AA;  56798 MW;  986EE45CF13A070A CRC64;
     MTLPLQDSIL IVDFGSQVTQ LIARRVREAG VYSEIAPFNN AAEAFERLKP KGIILSGGPS
     SVMWEDSPRA PQHFFDAGVP VLGICYGQQT MMQQLGGNVE GGESGEFGRA FIEVKKGCAL
     FDGLWSEGEK HQVWMSHGDK VTRLAPGFEV VAVSEGAPYA ITANEEKRFY ATQFHPEVVH
     TPDGAKLLAN FVRHVCGLKG DWTMAEFRAT KIADIRAQVG EGRVICGLSG GVDSAVAAVL
     IHEAIGDQLT CVFVDHGLMR LGEAEQVVSL FREHYGIKLV HVNAEERFLG GLAGLTDPEK
     KRKFIGGEFI AVFEEEAKKI GGADFLAQGT LYPDVIESVS FTGGPSVTIK SHHNVGGLPE
     RMNMKLVEPL RELFKDEVRV LGRELGLPEI FVGRHPFPGP GLAIRIPGEV SKERCDILRK
     ADAVYLEEIR NAGLYDAIWQ AFAVLLPVRT VGVMGDYRTY DSVCALRAVT STDGMTADIY
     PFDAAFLSRV ATRIINEVKG INRVVYDYTS KPPGTIEWE
//

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