ID A0A1H8X2C8_9PSEU Unreviewed; 1033 AA.
AC A0A1H8X2C8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:SEP34064.1};
GN ORFNames=SAMN04489732_106192 {ECO:0000313|EMBL:SEP34064.1};
OS Amycolatopsis saalfeldensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=394193 {ECO:0000313|EMBL:SEP34064.1, ECO:0000313|Proteomes:UP000198582};
RN [1] {ECO:0000313|EMBL:SEP34064.1, ECO:0000313|Proteomes:UP000198582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44993 {ECO:0000313|EMBL:SEP34064.1,
RC ECO:0000313|Proteomes:UP000198582};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOEF01000006; SEP34064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8X2C8; -.
DR STRING; 394193.SAMN04489732_106192; -.
DR Proteomes; UP000198582; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198582}.
FT DOMAIN 164..319
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 813..858
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1033 AA; 108297 MW; 670B85936790BB6F CRC64;
MPQDDTTPAE GNTPGSNTAD SRGNLSSGDE ASGGNSPSGG QPGGGDSLGG GQSGGQPNGG
KPSGGNVSSS DSSGGGQSGS KPSSGKPSSG KPSSGNEFSS DSPGGSKPAG QSGGGTNPAD
HQPGDQATAD RPVANDSDRK GLREPFDYPR DWEADVVLSD GGTVHLRPVV PSDADGLVAL
HGRLSERTRY FRYFGAYPRI PPRDLVRFST VDHHDRVAFA ALLGDDIVAV GRYERLDQGP
SAEVAFLVDD RHQGRGLGSI LLEHLAAAAS ESGLRRFVAE VLSENAAMVR VFRDAGYQVS
RAIEEGVLHL EFDIDPTEES LAVARSREQA AEARSVHNLL HPRSVAVIGA STDHMKVGHV
AFRNLLSADF TGTVYPVNPE HRSVRGVRAY PSVLDIPDPV DLALVAVPAE AVESVLDACL
AKGVKTLLIV SGGFGESGPL GLHAELRLVG EARAHGMRVV GPNALGVLNT AKDIRLNATL
APVLPKRGRT GFFCQSGALG TAILADAGSR GLGLSTFVSA GNRADVSGND LLQYWETDPE
TDLVLLYLES FGNPRKFARL ARRLGRSKPI VAVKSGRHAV RPQLAATSAE VDEASVKALF
EQAGVVRVES LAQLFDTALV FAHQPLPAGP RIGIVGNSIA IGLLAADTAR SQGLRLAFDP
VDIGPQAGPE EFAAAVREAL DSPDTDALIA VFAPPVAIPG AAYARALREA VVELKQSKPI
VSTFLAAEGV PDELAVLSDD GVPTRGSIPS YPSPERAVDA LARVVRYAAW RQRPQGALVR
PGGMHVEQAQ ELVRELLSDE EGHATLLSDD DVVRLLGCYG VAVVPFRVVS TVDDAVAAAA
ELGYPVTLKA VDERLRGRPD LAGVRLDLTS EDSVRVAYRD LREVSGEDDV YVQRMAPKGI
SCVIGLQDDP SFGTLVSFGL SGLVSTLLGD RAYRAVPLTD VDAATLIREP RTSPLLTGYR
GDEPADLAAL QDMVLRVAAL AEDNPEVRSL SLDPILASPD GAFVANARMV LGPPPSRPDT
GPRRLRHITP ADS
//