ID A0A1Q5RVV5_9BRAD Unreviewed; 739 AA.
AC A0A1Q5RVV5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:OKO79870.1};
GN ORFNames=AC629_28140 {ECO:0000313|EMBL:OKO79870.1};
OS Bradyrhizobium sp. NAS80.1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1680159 {ECO:0000313|EMBL:OKO79870.1, ECO:0000313|Proteomes:UP000186592};
RN [1] {ECO:0000313|EMBL:OKO79870.1, ECO:0000313|Proteomes:UP000186592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAS80.1 {ECO:0000313|EMBL:OKO79870.1,
RC ECO:0000313|Proteomes:UP000186592};
RA Granada C., Sant'Anna F.H., Passaglia L.;
RT "Genome of Bradyrhizobium sp. NAS80.1.";
RL Submitted (JUL-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:OKO79870.1}.
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DR EMBL; LGHL01000136; OKO79870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5RVV5; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000186592; 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: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 Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 522..558
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 739 AA; 77825 MW; 2DA060EA0F4EABDC CRC64;
MEAHVSAASV SPRPWSPPPD ASDIVKGIHA MLHPHNIVLV GATDKPGNYA ERIWNNLVKY
GYEGGLYPVN AKRETIWGVP CYKDFASLPE KPDHVLVLVP ARFAVQVIRD AAAAGARSAT
IVTSGFSELQ DDESQKLAAE LQAAVRETGL AVTGPNCLGN LSAGERLFTN IDDRIVTMDQ
GAVAIAGQSG AIVMAIRQAL EDRGVGVGYM VTTGNEAGLE TPDLMRYFAE DPSIKVIVVY
LEGVRNTKAF RDACKAARAA SKPVIALKLG ASEGGRAAAM AHTGALAGSI ETFDAIATRE
GVIRVGGLDE LIETTECFVH SEVPKGDRLA AVTLSGGKRG MLIDAFYAEG LNFAPLSPHV
SGELAKMLGP GSIVGNPLDA GFAAVVDPSV YMKSIKLMID DPDIDIVIVD SELPKAPHEQ
RERNLRIVNE MASRASKPVI YISAMSIGFT EFTKTLRKSL PHLAVMQGMD RAVTAIKSLL
DYAKLRKEVP DIVSSSKPAA RAVLEKTLKS ASGAALDEVA SKKLLKAYGI PISKEAIAQT
APEAVKIAKQ IGFPVVAKVV SAEILHKSDI GGVVLNLNNA TDVKKAFADI TARVKKLKGK
PKLDGILIAQ QVKADLELVV GASLDAEMGP VVLFGTGGID IELMKDVALA GAPLDEAEAR
ILVGRTKAGI KMCGYRGKPA LHEASAVKAL VGLSNLIADA GDRIASIDIN PFLINTKTGV
AVDALIVLNN AAAKRAAGH
//
