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Database: UniProt
Entry: A0A1H8X2C8_9PSEU
LinkDB: A0A1H8X2C8_9PSEU
Original site: A0A1H8X2C8_9PSEU 
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.
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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
//
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