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Database: UniProt
Entry: A0A1Q3JXW7_9SPHI
LinkDB: A0A1Q3JXW7_9SPHI
Original site: A0A1Q3JXW7_9SPHI 
ID   A0A1Q3JXW7_9SPHI        Unreviewed;       314 AA.
AC   A0A1Q3JXW7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   SubName: Full=5-(Carboxyamino)imidazole ribonucleotide synthase {ECO:0000313|EMBL:OJU25651.1};
DE   Flags: Fragment;
GN   ORFNames=BGN92_01145 {ECO:0000313|EMBL:OJU25651.1};
OS   Sphingobacteriales bacterium 41-5.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895836 {ECO:0000313|EMBL:OJU25651.1, ECO:0000313|Proteomes:UP000187304};
RN   [1] {ECO:0000313|EMBL:OJU25651.1, ECO:0000313|Proteomes:UP000187304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=41-5 {ECO:0000313|EMBL:OJU25651.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
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:OJU25651.1}.
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DR   EMBL; MKRO01000136; OJU25651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3JXW7; -.
DR   Proteomes; UP000187304; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   PANTHER; PTHR11609:SF5; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR   PANTHER; PTHR11609; PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7; 1.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF17769; PurK_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT   DOMAIN          43..225
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OJU25651.1"
SQ   SEQUENCE   314 AA;  35178 MW;  EDF918CDD7D26BA3 CRC64;
     LDAITIEIEN VNIDALEQLE KEGKRIYPRP SVLRIICNKA LQKEYYSSNQ IPTSAYILTN
     NLSELVANKD FLPAVHKLAE GGYDGRGVQV INDENDIEKG FNQLSVLEKL VDVSKEIAMM
     IAVSDSGETA IYPPVEMMFD RDLNQLDLQL CPAEIEDRVY WKLEAIALTT VKNFKSSGIF
     AVEMFVTPEG DVLVNETAPR VHNSGHHSIE AHFSSQFDML WRVILNYPLG NTDAIKNSVM
     VNITGAAGEQ GPAYYEGLEE MLKIENAFFH IYGKRQTKPG RKMGHVTILS NEKADLMHKA
     NKIKHGLKVI ATKI
//
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