ID A0A0Q5VDI6_9ACTN Unreviewed; 645 AA.
AC A0A0Q5VDI6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN ORFNames=ASG36_00370 {ECO:0000313|EMBL:KQS59565.1};
OS Geodermatophilus sp. Leaf369.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS59565.1, ECO:0000313|Proteomes:UP000051830};
RN [1] {ECO:0000313|EMBL:KQS59565.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS59565.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS59565.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS59565.1,
RC ECO:0000313|Proteomes:UP000051830};
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:KQS59565.1}.
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DR EMBL; LMQA01000001; KQS59565.1; -; Genomic_DNA.
DR RefSeq; WP_055757953.1; NZ_LMQA01000001.1.
DR AlphaFoldDB; A0A0Q5VDI6; -.
DR STRING; 1736354.ASG36_00370; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000051830; Unassembled WGS sequence.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:InterPro.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
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; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051830}.
FT DOMAIN 20..71
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 77..459
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 522..601
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 645 AA; 69338 MW; DC2059FCACF888FA CRC64;
MTGYPPPPEF AARANVGPDA HAHAEADAFA FWAEQAGRLQ WDTPWDTVFD DGEMPTARWF
TGGRLNVAVN CVDRHVTAGR GDDVALHWVG EPGDGRTVTW AQLQDDVCRL ANALTALGIE
AGDRVVLYLP VLVETVVATL ACARIGAVVS LVFGGFSADA LRFRVADTGA KLLIATDGQF
RRGSAVAVKA TADEAVAGLD HVEHVLVVRR TGETDVPWTP GRDLWWHELL AEQSPVHEPA
SFDAEHPLFI VYTSGTTGRP KGLVHTSGGY LTQASWTHWA LFDAKDDDVY WCQADLAWVT
AHTYVLYGPT SNGTTQVLYE GSPLTPHPGR HFEVIAGLGV TVYYTAPTLV RTFMKHGPEL
PAGYDLSSLR LLGSVGEAIN PEAWRWLHEH VGGGRCPIVD TWWQSETGAA VIAPLPGVTV
LEPGSATVPL PGLAAAVVDD AGRPTPPGVE GNLVITRPWP AMARTVWRDH ARFVASYWAP
YAEQGWYLAG DSASVDEAGY VWIGGRIDDV LNVSGHRLSS IELESALVSH PRVAEAAVVG
APDDVTGQRI VAFVITRDDA GADDTGLTEE LRAHVARRVG AIAKPREVVV VTDLPKTRSG
KIMRRLMADM TAGRGGGDTT SLTDPGSMTT VERAWDAHAA LRDRT
//
