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Database: UniProt
Entry: A0A0Q6VGZ9_9ACTN
LinkDB: A0A0Q6VGZ9_9ACTN
Original site: A0A0Q6VGZ9_9ACTN 
ID   A0A0Q6VGZ9_9ACTN        Unreviewed;       646 AA.
AC   A0A0Q6VGZ9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Acetoacetyl-CoA synthetase {ECO:0000313|EMBL:KQV74451.1};
DE            EC=6.2.1.16 {ECO:0000313|EMBL:KQV74451.1};
GN   ORFNames=ASC61_05230 {ECO:0000313|EMBL:KQV74451.1};
OS   Aeromicrobium sp. Root344.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736521 {ECO:0000313|EMBL:KQV74451.1, ECO:0000313|Proteomes:UP000051702};
RN   [1] {ECO:0000313|EMBL:KQV74451.1, ECO:0000313|Proteomes:UP000051702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root344 {ECO:0000313|EMBL:KQV74451.1,
RC   ECO:0000313|Proteomes:UP000051702};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV74451.1, ECO:0000313|Proteomes:UP000051702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root344 {ECO:0000313|EMBL:KQV74451.1,
RC   ECO:0000313|Proteomes:UP000051702};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQV74451.1}.
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DR   EMBL; LMDH01000001; KQV74451.1; -; Genomic_DNA.
DR   RefSeq; WP_056210175.1; NZ_LMDH01000001.1.
DR   AlphaFoldDB; A0A0Q6VGZ9; -.
DR   STRING; 1736521.ASC61_05230; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000051702; Unassembled WGS sequence.
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   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; 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   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:KQV74451.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051702}.
FT   DOMAIN          30..84
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          96..463
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   646 AA;  69962 MW;  E370BB591D2A110C CRC64;
     MTDILWSPPL DGASRLERFM QELDQPFADY DALWAWSVEQ PNDFWRAAWR HFDVPSDGDP
     TSALADASMP GAVWFPDVRL NYAEAMLRLP GRGDDDVVVV AASQSRDDVR LTARELRDQV
     GRARAGLQRA GVRTGDRVAA YAPNIPETLV LLLAAASLGA VFSSCAPEFG TQSVVDRWQQ
     IEPTILLAVD GYRYGAKGVD RRAEVEAITG SLPSLRTVVW LPYLDAEAPA PGGAVTWAEL
     TAETGPLEFV RLPFAAPLYV LFSSGTTGLP KPIVHGHGGI TLEHLKSLAF HHDLGPADRF
     FWFSTTGWMM WNLLISGLAV GSTIVMFDGN PAHPDLGMLW QLAERLEMTY FGTSAPFLLQ
     CRKEGLVPRE TADLSRLRGV GSTGAPLPAE GFRWVYDAVS ATAQLGSISG GTDVCSGFVG
     AAPIVPVYAG EISCRMLGCA VEAYDDERRP VTGSLGELVI TQPMPSMPVG FWGDTDGSRY
     RAAYFEDIPG VWRHGDWITI SERGTCVITG RSDATLNRGG VRLGTAEFYT VVEALPEVVD
     SLVVHLEDDE GGAGQLLLFV VLAERLDLDE ALHQRIAIAL RTQLSPRHVP DAIRQVAALP
     RTLSGKKLEV PVKKILQGAS IEDAAAKGAL TDPTSLDAFV TIRETL
//
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