ID V4J3Z2_9GAMM Unreviewed; 397 AA.
AC V4J3Z2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|ARBA:ARBA00021562};
DE AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356};
DE Flags: Fragment;
GN ORFNames=N838_20880 {ECO:0000313|EMBL:ESQ09129.1};
OS Thiohalocapsa sp. PB-PSB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiohalocapsa.
OX NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ09129.1, ECO:0000313|Proteomes:UP000017935};
RN [1] {ECO:0000313|EMBL:ESQ09129.1, ECO:0000313|Proteomes:UP000017935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA Orphan V.J.;
RT "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT consortia of the Sippewissett salt marsh.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESQ09129.1}.
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; AVFR01001277; ESQ09129.1; -; Genomic_DNA.
DR AlphaFoldDB; V4J3Z2; -.
DR Proteomes; UP000017935; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00888; guaA_Nterm; 1.
DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Reference proteome {ECO:0000313|Proteomes:UP000017935}.
FT DOMAIN 207..397
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 85
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 234..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
FT NON_TER 397
FT /evidence="ECO:0000313|EMBL:ESQ09129.1"
SQ SEQUENCE 397 AA; 43562 MW; 42282044CB7CDCC7 CRC64;
MRNIHADRIL ILDFGSQYTQ LIARRVREAG VYCELHPWDM PADRIHDFAP KGVILSGGPR
SVHENATPRA DPLIFDLGVP LLGICYGMQA MAAQLGGSVV AASEREYGYA QVRARGHSRL
LRDIEDHTSP EGYGLLDVWM SHGDRVDALP NGFKVIATTD NAPFAGIADE ARSFYGVQFH
PEVTHTRQGK RIVERFCHEI CGCGNLWTSS NIIDDAIAQV RAQVGDDEVL LGLSGGVDSS
VVAALLHRAI GAKLLCVFVD NGLLRLGEGD QVMATFARHL GLRVIRVDAE AHFLEQLAGI
KDPEQKRKRI GNTFIEVFNQ QAAKLSNIKW LAQGTIYPDV IESAGAKTGK AKVIKSHHNV
GGLPEHMQLG LVEPLRELFK DEVRQLGVQL LSLIHIS
//
