ID A0A0J5T2C8_9RHOB Unreviewed; 383 AA.
AC A0A0J5T2C8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Adenylosuccinate synthetase/AAA domain {ECO:0000313|EMBL:KMK64217.1};
DE EC=6.3.4.4 {ECO:0000313|EMBL:KMK64217.1};
DE Flags: Fragment;
GN ORFNames=IMCC21224_141 {ECO:0000313|EMBL:KMK64217.1};
OS Puniceibacterium sp. IMCC21224.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Puniceibacterium.
OX NCBI_TaxID=1618204 {ECO:0000313|EMBL:KMK64217.1, ECO:0000313|Proteomes:UP000036046};
RN [1] {ECO:0000313|EMBL:KMK64217.1, ECO:0000313|Proteomes:UP000036046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC21224 {ECO:0000313|EMBL:KMK64217.1,
RC ECO:0000313|Proteomes:UP000036046};
RA Cho J.-C., Yang S.-J., Kang I.;
RT "Complete genome sequence of IMCC21224 belonging to the
RT Alphaproteobacteria.";
RL Submitted (MAY-2015) 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:KMK64217.1}.
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DR EMBL; LDPY01000004; KMK64217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J5T2C8; -.
DR STRING; 1618204.IMCC21224_141; -.
DR PATRIC; fig|1618204.4.peg.4841; -.
DR OrthoDB; 5524039at2; -.
DR Proteomes; UP000036046; Unassembled WGS sequence.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.440.10; Adenylosuccinate Synthetase, subunit A, domain 1; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1.
DR PANTHER; PTHR11846:SF0; ADENYLOSUCCINATE SYNTHETASE; 1.
DR Pfam; PF13238; AAA_18; 1.
DR Pfam; PF00709; Adenylsucc_synt; 2.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KMK64217.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000036046}.
FT NON_TER 383
FT /evidence="ECO:0000313|EMBL:KMK64217.1"
SQ SEQUENCE 383 AA; 41893 MW; D121F7A6C137FDC3 CRC64;
MKHIIVTSGP IGVGKSLFSA EIEKRPKVKR VSTRKHILEA MKCENERGAL QRAGDKLDVE
SDGKWVADAV ENAINNDSSV EIFLVDSARI ESQVTELRNR FGGAVFHIHL TAADEELERR
YKLRKQELKE YLTYQEAASH GTERGVKDLA SVADLCLNTD HVDAESLATA ALAWRGFSSK
PYDPEQLVDV IVGGQYGSEG KGNVCAAIAT DYAALVRIGG PNAGHKVAVP EYTFVQLPSG
TGSTPDAEIM IGAGSTISLP KLLKEILDQK LDGERLSIDP RAMIINDWDR EIEQKGLQKI
STTGQGVGAA SSRKILNRDN ETFGPAVRLA GEVSELKEYV RNVRLRIEKI LERGGRILIE
GTQGTMLSIH HGLYPHVTSR ETS
//
