ID A0A3E2YJH4_9ACTN Unreviewed; 626 AA.
AC A0A3E2YJH4;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetyl-coenzyme A synthetase {ECO:0000313|EMBL:RGC66472.1};
DE EC=6.2.1.1 {ECO:0000313|EMBL:RGC66472.1};
GN Name=acsA3 {ECO:0000313|EMBL:RGC66472.1};
GN ORFNames=C5N14_24040 {ECO:0000313|EMBL:RGC66472.1};
OS Micromonospora sp. MW-13.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2094022 {ECO:0000313|EMBL:RGC66472.1, ECO:0000313|Proteomes:UP000258607};
RN [1] {ECO:0000313|EMBL:RGC66472.1, ECO:0000313|Proteomes:UP000258607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW13 {ECO:0000313|EMBL:RGC66472.1,
RC ECO:0000313|Proteomes:UP000258607};
RA Jahanshah G., Miess H., Busche T., Ruckert C., Kalinowski J.,
RA Rokni-Zadeh H., Gross H.;
RT "Draft Genome Sequence of Micromonospora sp. MW-13, a Bacterical Strain
RT Isolated from the Rhizosphere of Wheat in Iran with antibacterial and
RT possibly plant growth promotion properties.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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:RGC66472.1}.
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DR EMBL; QKKX01000054; RGC66472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2YJH4; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000258607; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR CDD; cd05967; PrpE; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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 PANTHER; PTHR43347; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43347:SF3; ACYL-COA SYNTHETASE SHORT-CHAIN FAMILY MEMBER 3, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:RGC66472.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000258607};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 113..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..58
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 62..446
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 511..589
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 626 AA; 67131 MW; AB5BDE9135AE8B1B CRC64;
MGAYRAAYER SIADPTAFWR DAAADIDWHR PPERILDDGR APLYRWFPDG ELNTCHNALD
RHVAAGRGDQ AALIHDSPVT GTTRTYTYAE LRDATARFAG ALRRLGVGRG DRVLLYLAMV
PEAVVAMLAC ARIGAVHSVV FGGFAAHELA VRVDDARPKV VVATSCGIEA DRVVPYHPIL
DAALAEAEHA PERCVIVQRP QHPAPLTPGR DLTWDEALDG AEPADCVPVA ATDPLYVLYT
SGTTGRPKGV VRDNGGHAVA LRWSMTNVFG IGPGDVFWAA SDVGWVVGHS YIVYGPLLTG
ATTVLYEGKP VGTPDAGAFW RVVSQHRVAA LFTAPTAIRA IRRQDPDGTR IGRYDLSSLR
TLFLAGERLD PDTFAWAGAR LGVPVVDNWW QTETGWPVAA NPRGLEPLPI KAGSPSVPVP
GYDVRVVDPR GAQVPAGVDG SIVIRLPLPP GCLPTLWGDD ERYVRSYLST FPGHYLTGDG
GRFDDDGYLY VMGRTDDVIN VAGHRLSTGA MEEVLAGHPA VAECAVIGVS DQLKGQVPSG
YVVLKAGVEV EPAALAAELV ARVRERIGPV AAFRRVTVVP ALPKTRSGKI LRRTMRGLVE
GRDEPVPATI DDPATLGVFR DLAAAD
//
