ID A0A0Q4V3I6_9MICO Unreviewed; 668 AA.
AC A0A0Q4V3I6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN ORFNames=ASF23_10565 {ECO:0000313|EMBL:KQO62248.1};
OS Curtobacterium sp. Leaf261.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO62248.1, ECO:0000313|Proteomes:UP000050821};
RN [1] {ECO:0000313|EMBL:KQO62248.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO62248.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO62248.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO62248.1,
RC ECO:0000313|Proteomes:UP000050821};
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:KQO62248.1}.
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DR EMBL; LMMJ01000009; KQO62248.1; -; Genomic_DNA.
DR RefSeq; WP_055953773.1; NZ_LMMJ01000009.1.
DR AlphaFoldDB; A0A0Q4V3I6; -.
DR STRING; 1736311.ASF23_10565; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000050821; 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 CDD; cd05966; ACS; 1.
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:UP000050821}.
FT DOMAIN 49..103
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 111..500
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 553..634
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 72151 MW; 2A46A583F3A5AC1F CRC64;
MTTPTEAHAR PGRSDASGST APSGDGSVDG GRTSYPPSAA FVAGAVAHED LHHAAEADRL
QFWADQSREL LDWRTPFTRT LDFDDAPFAK WFDDGTLNVA ENCLDRHVRN GLGDRVAIHF
EGEPGDTRTI TYAELTADVQ RAANMLSDLG VVAGDRVVVY MPLIPEAVVA MLAVARLGAI
HSVVFGGFSA ESLRARIEDA GAKLVVTADG GWRKGAVAPL KPAVDEALEG EGTDSIEHVL
VVRRGGNDVT WNERDLWWHD EMAKAAPEHE ARAFPSEQPL FILYTSGTTG KPKGIVHTSG
GYLTQAAFTH RNVFDMHPET DVYWCTADIG WITGHSYVVY GPLANGVTQV LYEGTPDVPE
PGRWWDLVDK YGVTVLYTAP TAVRSAMKAG RQIPDARDLS SLRLLGSVGE PINPEAWHWF
RQVIGHDRTP VVDTWWQTET GAIMVSALPG VTQLKPGAAQ CPIPGILAEV VDEDGNRVEP
GASGLLTIAE PWPSMARGIW HDPDRFIETY WSKFPGRYFA GDGARLDGEG DIWLLGRVDD
VMNVSGHRLS TAEIESALVE HDGVAEAAVV GADDKTTGQA IVAFVILTAA AADGVDRAAV
SEELRQFVGQ RIGAIARPRQ VVIVPELPKT RSGKIMRRLL RDAAEGRTVG DTTTLADGGI
MAQITELM
//
