ID A0A0S2K3J7_9GAMM Unreviewed; 893 AA.
AC A0A0S2K3J7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Acyl-CoA synthetase, NAD(P)-binding protein, ATP-binding protein {ECO:0000313|EMBL:ALO42908.1};
GN ORFNames=PP2015_2416 {ECO:0000313|EMBL:ALO42908.1};
OS Pseudoalteromonas phenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO42908.1, ECO:0000313|Proteomes:UP000061457};
RN [1] {ECO:0000313|EMBL:ALO42908.1, ECO:0000313|Proteomes:UP000061457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO42908.1,
RC ECO:0000313|Proteomes:UP000061457};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013187; ALO42908.1; -; Genomic_DNA.
DR RefSeq; WP_058030609.1; NZ_CP013187.1.
DR AlphaFoldDB; A0A0S2K3J7; -.
DR STRING; 161398.PP2015_2416; -.
DR KEGG; pphe:PP2015_2416; -.
DR PATRIC; fig|161398.10.peg.2467; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000061457; Chromosome I.
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:UniProtKB-KW.
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; 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;
KW ATP-binding {ECO:0000313|EMBL:ALO42908.1};
KW Nucleotide-binding {ECO:0000313|EMBL:ALO42908.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000061457}.
FT DOMAIN 734..889
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 893 AA; 97882 MW; F5033BC316CAA29C CRC64;
MSVKRISQFF NPKSVAVIGA SNNAGRAGFV VMRNLLQGGF KGPIMPVSPK HKAVHGVLAY
HNIKALPQTP DLAVICTNKN TLKQIIIELG ELGCQHAIII ASGANQAQKS ALKQTAKEAG
VTLLGPNCLG LLIPHLGLNA SFSHTVAEPG KLAFISQSAA VCSTILDWAQ NKRIGFSYFI
SVGDCIDIDF DELLDFLGRD AKTRAILLYI DNIDDVRRFI SAARAAAFSK PVLVIKTGRT
RAGAEAAYIH TGGQSSDDAV YDAMFQRAGM LRVNDLRELF AATQTLALHP KLLQVEQLTI
LTNGGGPGIM AVDTLLQGSG KLAELSDQTR EALNKVIPQA EKIYNPVDLF GDSSPKRYQQ
ALEILLKAPE VKNLLIIHTP SALAPSEEYA EIIANALEKI PKMARPYVMT VFMGEYAAYE
ARYVCAEHSI PTYRTPEGAV GAFMHLVSYR RNQKHLTQTP ESISSDLLIN SQAAKHEIAE
FIAEGHTHLS THLARKVLSH YSIECIQTEI ALTPSEAKEQ AERLGFPVAL KLISPSIPSK
SEVGGVVLNL NDGNEVEQNA FAILLRIKEA YPDAIIEGFS LQRMAPRAGA QELRIAIKTE
PGFGPVILLG EAGTGLEFSQ AAVALPPLNM NLAKYLIAAA QDKGVLKERT LPDKVDKYRL
CALLTRISQL LVDQPDIYNL ELNPVLASEG QFLVLDAAIQ LRPYQVKANR KRLAIKPYPK
EWEQKVTLKD GQAAVLRPIR PEDERAHQEF DQSLTKEDRY KRFFGELPEF NHEQLAKMTQ
IDYDREMAFI VSAPHKSAYR TLGVSRVLMD PDNLSAEFAV VVRSGSQGLG LGKLLMNAAI
DYCRSQGVGV VEGITLPENT GMIELSKRLG FKVTRDFEEG TINMVLKLDE AQQ
//