ID G2KQ38_MICAA Unreviewed; 669 AA.
AC G2KQ38;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Acetoacetate-CoA ligase {ECO:0000313|EMBL:AEP08580.1};
DE EC=6.2.1.16 {ECO:0000313|EMBL:AEP08580.1};
GN OrderedLocusNames=MICA_234 {ECO:0000313|EMBL:AEP08580.1};
OS Micavibrio aeruginosavorus (strain ARL-13).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Micavibrio.
OX NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP08580.1, ECO:0000313|Proteomes:UP000009286};
RN [1] {ECO:0000313|EMBL:AEP08580.1, ECO:0000313|Proteomes:UP000009286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARL-13 {ECO:0000313|EMBL:AEP08580.1,
RC ECO:0000313|Proteomes:UP000009286};
RX PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA Wang Z., Kadouri D., Wu M.;
RT "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT aeruginosavorus ARL-13.";
RL BMC Genomics 12:453-453(2011).
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DR EMBL; CP002382; AEP08580.1; -; Genomic_DNA.
DR AlphaFoldDB; G2KQ38; -.
DR STRING; 856793.MICA_234; -.
DR KEGG; mai:MICA_234; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_3_5; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000009286; Chromosome.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd05943; AACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR005914; Acac_CoA_synth.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR01217; ac_ac_CoA_syn; 1.
DR PANTHER; PTHR42921; ACETOACETYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR42921:SF1; ACETOACETYL-COA SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEP08580.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009286}.
FT DOMAIN 54..109
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 112..490
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 561..631
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 73925 MW; 22F2A8B7CC24B3B3 CRC64;
MGQAKMTKTD RDAVITKNGN GPLWSPDRVR RDRSSLHHFM ERAEVRAGQE FSDYDSIWRW
SVDNTESFWD LVWDACGVIG DKGATILQDG DRMPGATFFP DARVNYAENL LRRRDDAVAM
IFRNEKGEER QLSFNDVYDL SSQIAQALHH AGVGEGDRVA AFMPNTPETI IAMLAATSLG
AIWSSASPDF GVQGLVDRFG QIEPKVLFAV DAYYYNGKTV DCLHRVAEVQ PRLPGLQCTV
IVPFVNPNPD LTGLDRAVTL GDFVAPFVPR DMYFNRVAFN HPLFIMFSSG TTGIPKCIVH
GHGGTLIQHL KEHQLQCDIG EGDRVFYFTT CGWMMWNWLV SALASGCTLM LFDGSPFYPN
GKTLWDFAEK HSCTLFGTAA KYIDALKAAG LRPGDEHDLS ALRVITSTGS PLVHESFDYI
YDAIKKDVHL ASISGGTDII SCFVLGNPLS PVWRGEIQGP GLGMAVDAFD EDGKPIPAGA
GSGELVCTKP FPSMPVMFWN DHDGAKYHAA YFERFDNVWC HGDWIERTNH GGFIIHGRSD
ATLNPGGVRI GTAEIYRQVE QIPEVIESIA VGQDWDNDVR VVLFVRLRDG VTLSGELADR
IKAQIRAGAS PRHVPARIIA VTDIPRTKSG KITELAVRDI IHGRKVKNVE ALANPEALDL
YKDLPELKA
//
