ID A0A0F7FYV6_9ACTN Unreviewed; 905 AA.
AC A0A0F7FYV6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:AKG45964.1};
GN ORFNames=SXIM_45800 {ECO:0000313|EMBL:AKG45964.1};
OS Streptomyces xiamenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG45964.1, ECO:0000313|Proteomes:UP000034034};
RN [1] {ECO:0000313|Proteomes:UP000034034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA Xu J.;
RT "Complete genome sequence of a mangrove-derived Streptomyces xiamenensis.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP009922; AKG45964.1; -; Genomic_DNA.
DR RefSeq; WP_046724999.1; NZ_CP009922.3.
DR AlphaFoldDB; A0A0F7FYV6; -.
DR STRING; 408015.SXIM_45800; -.
DR KEGG; sxi:SXIM_45800; -.
DR PATRIC; fig|408015.6.peg.4635; -.
DR HOGENOM; CLU_007415_3_0_11; -.
DR Proteomes; UP000034034; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
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; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR000182; GNAT_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; 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; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 25..193
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 688..726
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 905 AA; 94745 MW; FC6F800A4FDEDCE7 CRC64;
MRTPEQPVYP AHWEADVVLR DGGTARIRPI TPADAERLVR FYERVSDEAK YYRFFAPHPR
LSDKDVHRFT HHDYDDRVGL AATVGDDFLA TVRYDRVDRH GNPASRSHPP AGDAPVADRA
EVAFLVEDAH QGRGLASVLL EHIAAVARER GIRRFEAEVL PANSKMIKVF TDAGYSQRRS
FAGGSVHLTL DLEPTAASLA VMRAREQRAE ARSLQRLLAP RSIAVVGAGR APGGAGRLVL
DRLRAGGFAG PLYAVNRALP EDTTEIDGIP AHRSLREIPG PVDLAVLAVP ADRVDQVLTD
CGEHGVQGLL VLSTGHTGQA QRALVRRARS YGMRLIGPGA FGVLNTAPGV RLNASPAPYL
PPPGRIGVFT QSAAIAITVL EELEGSGAGL SSFISAGNRA DLSGNDALQF WDEDPDTHVV
LMYLESLGNP RKFTRLARRT AAAGKPVVVV RGGRHSGGAL PPGHVVPATS TPEDTAAALI
RQAGVIEADT VTELVDTGVL LAGQPLPPGH RIAVLGNAEA LGLVAHDACR AQDLSPLPTT
ALPPDAGPED YRHALGTALA DPDTDAVVVT AVPTGGAGLT APALTDALHA AITAVPGRRI
PVVVAHLAID GLATALSARG IPGYPSAERA VRALAHAVRH ARWRADAAVP GSVPAFDDID
EHAATRVIAA ASAGEAAGRH PLATDRAQRL LATYGITVLP ALAAPGPDAA VRAARRLGFP
VALKATAPGL RHRADLDGVR LGLATEGELR RAHAELAALG SHDAPRPVVQ AMAPRGVDTV
VRAVADPAIG AVLSFGLAGP ASELLGDIAH RLLPVTDRDV AALVRSIRAA PMLFGWRGAS
PVDTDALEEL LLRLGRLVED HPEIAAVTLE PVVVAPRGLS VLAATVALAP PSPSPDLAPR
RLPAY
//