ID A0A1C6MAD2_9ACTN Unreviewed; 925 AA.
AC A0A1C6MAD2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:SCK15759.1};
GN ORFNames=H180DRAFT_01049 {ECO:0000313|EMBL:SCK15759.1};
OS Streptomyces sp. WMMB 322.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1286821 {ECO:0000313|EMBL:SCK15759.1, ECO:0000313|Proteomes:UP000182082};
RN [1] {ECO:0000313|EMBL:SCK15759.1, ECO:0000313|Proteomes:UP000182082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMB 322 {ECO:0000313|EMBL:SCK15759.1,
RC ECO:0000313|Proteomes:UP000182082};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMHI01000002; SCK15759.1; -; Genomic_DNA.
DR RefSeq; WP_055484773.1; NZ_FMHI01000002.1.
DR AlphaFoldDB; A0A1C6MAD2; -.
DR STRING; 1286821.GCA_001418285_01047; -.
DR OrthoDB; 190266at2; -.
DR Proteomes; UP000182082; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR043938; Ligase_CoA_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF19045; Ligase_CoA_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
FT DOMAIN 21..173
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 833..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 925 AA; 96620 MW; 31F9E91AD046D0D0 CRC64;
MTYAAPRMAE TYALLTDGRT VQIRPARPSD RGQVEALYEG MSQQDHKQRF FGAGAGLRER
EIDRVFGPGR SDLLVLLALH GSQLIGTAEY EKLLEEPAAA EIALAVADGF QHCGVGTLLL
EHLAHAARAE HITTFTADAL AENRDVLDVF ENLGLRYERT FENGEVRCRV DLTPHESYLA
AVDARGSTAD VASMRPLLQP RSVAVVGAGR SPKSVGRAVL RNLRRSGFTG AVHGINPHAA
SIEGFACRPA VSELPHTPDL AVIAVPAHAV PEAADQCGRF GVRALTVLTS GLDEALGGAL
LDICRHYGMR LVGPDCLGIA NTEDGIRLDA TFAADLPEPG TAGVAVQSGG VGIALLSDLA
RLGIGVSSFV SLGDKYDVSG NDLLQWWEAD ERTRVGLLHL ESFGNPRAFS RTARRVTRLM
PVLTVDAGRS DAGRRAAAGH TAAAATPAMT RQALFHQAGV TATLSLGDLT ATAALMHSQP
LPTGTSVAVV SNAGGTGVLT ADACDEAGLT LPELPEDVAA ELRTLLPEAA RVANPLDTTA
AVGRGALAEC VELLSTRAPV DAVLVVLVPT ATAAAGGDDL VRAAASAEAP GGGRTLVTVL
PDQSERVRLV RTPGGTGPAA VPAYADPQDA ARALAHAAAR SRWLAHPPGH VPDLSGRVDT
DRARTLVQAA LSEHPEGTWL DPDRCGHLLD LYGIPRVPQS VVRDRAGAVR EAARLAPGGG
RLALKAYGPD LLHKSAHGAV VLDLEGPDAA GGAFRDLRNR LGERMDGAIV QPMAGRGVEL
IAGVVQDDVF GPLVLFGLGG TATDVLADHA ARLAPLTDRD VHELVAAPLC APTLRGQGQG
QGQGQGRGRG RGSGEAVDLP ALEDLLLRVS KMADDLPELA EADLNPVLAR PDGVAVLDCR
IRLAHPRPPR PGRGTGPHAY PRRLR
//