ID A0A1I7FHE3_9BRAD Unreviewed; 739 AA.
AC A0A1I7FHE3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:SFU35597.1};
GN ORFNames=SAMN05192541_101463 {ECO:0000313|EMBL:SFU35597.1};
OS Bradyrhizobium arachidis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=858423 {ECO:0000313|EMBL:SFU35597.1, ECO:0000313|Proteomes:UP000199591};
RN [1] {ECO:0000313|EMBL:SFU35597.1, ECO:0000313|Proteomes:UP000199591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26795 {ECO:0000313|EMBL:SFU35597.1,
RC ECO:0000313|Proteomes:UP000199591};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FPBQ01000001; SFU35597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7FHE3; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000199591; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR043938; Ligase_CoA_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF19045; Ligase_CoA_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Transferase {ECO:0000313|EMBL:SFU35597.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 522..558
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 77522 MW; 5EDA9DE253D63D4E CRC64;
MEAQVPAAST SPRPWSPPPD ASDVVKGIHA MLHPHNIVLV GATDKPGNYA ERIWNNLVKY
GYEGGLYPVN AKRETIWGVP CYKDFASLPE KPDHVLVLVP ARFAVQVIRD AAAAGARSAT
IVTSGFSELQ DAESQKLAAE LQAAVRETGL AVTGPNCLGN LSAGEKLFTN IDDRIVTMEQ
GAVAIAGQSG AIVMAIRQAL EDRGVGVGYM VTTGNEAGLE TPDLMRYFAE DPSIRVIVVY
LEGVRNTKAF RDACKAARAA SKPVIALKLG ASEGGRAAAM AHTGALAGSI ETFDAIATRE
GVIRVGGLDE LIETTECFVH SAVPKGDRLA AVTLSGGKRG MLLDAFYAEG LNFAPLSPHV
GSELAKMLGP GSIVGNPLDA GFAAVVDPSV YMKSIKLMID DPDIDIVIID AELPKAPHEL
RERNLRIVNE MASRASKPVI YISAMSIGFT EFTKSLRKSL PHLAVMQGMD RAVTAIKSLL
AYASLRKEVP DIVSSSKPAA RAMLEKALKA ANGAALDEVA SKKLLKAYGI PISKEAIAQT
AAEAAKIAKQ IGFPVVAKVV SAEILHKSDI GGVVLNLNSA AEVKKAFADI SARVAKLKGK
PKLDGILIAQ QVKADLELVV GASLDAEMGP VVLFGTGGID IELMKDVALA GAPLDEAEAR
LLIGRTKAGI KMRGYRGKPA LHETSAVKAL VGLSNLIADA GDRIASIDIN PFLINAKTGV
AVDALIVLNN AAAKRAAGH
//
