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Database: UniProt
Entry: F1W0A6_9BURK
LinkDB: F1W0A6_9BURK
Original site: F1W0A6_9BURK 
ID   F1W0A6_9BURK            Unreviewed;       881 AA.
AC   F1W0A6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Protein acetyltransferase {ECO:0000313|EMBL:EGF31723.1};
GN   ORFNames=IMCC9480_3496 {ECO:0000313|EMBL:EGF31723.1};
OS   Oxalobacteraceae bacterium IMCC9480.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae.
OX   NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF31723.1, ECO:0000313|Proteomes:UP000004494};
RN   [1] {ECO:0000313|EMBL:EGF31723.1, ECO:0000313|Proteomes:UP000004494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF31723.1,
RC   ECO:0000313|Proteomes:UP000004494};
RX   PubMed=21572000; DOI=10.1128/JB.05088-11;
RA   Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT   "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT   betaproteobacterium isolated from the Arctic Ocean.";
RL   J. Bacteriol. 193:3421-3421(2011).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGF31723.1}.
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DR   EMBL; AEPR01000371; EGF31723.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1W0A6; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000004494; 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:UP000004494};
KW   Transferase {ECO:0000313|EMBL:EGF31723.1}.
FT   DOMAIN          489..525
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          725..879
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   881 AA;  93650 MW;  2F82C4ACC97E48FE CRC64;
     MSIRHLQALF NPASVALIGA TNRPGSIGNA VLHNLVAGGF AGRIMPVNPK HEVLAGLIVW
     NDVASLPVVP DLAIICTPPA SVPELIAALG ERGCKAVIVM SAVTTAQREA MLLAAKPHLL
     RILGDISAGL LVPAIGLNAS FSSGPALPGK LAFVSQSGGL MNGVLDWATT RGLGFSKFIS
     LGGGADIDFG DLLDFLAGDP ATHAILLFLE DIRLARKFMS AARSAARGKP ILVIRAGRSG
     EGQRAGASHT GVLASPDSIY DAAIRRAGML RVNSTEALFG AVETLARAKP MHGERLTILT
     NGGGPGIMAN DALLGLNGRL ATLTPKSVTA LAQVLPSSWS QTNPVDLGGD APVERYRDAL
     AVLLNDANSD AILFIHAPGA LVSSTDIARA LVPLMKQSSR NVLTCWLGGA AVSVARQLCS
     AAGIATYDTP EEAVRGFMQI IDFRHNQQLL MQVPPALLDH GTTGRLRAQA LVRAALADGR
     TLLSEPETKI ILAAYGIPVV ETSTAATVDE AVLQAQRIGF PVAIKILSPQ IWHKSDVGGV
     ALDLEDADAV RHAARAMHKR LCELQPDAEL QGFAVQAMAR RPQAHELIVG VSTDPVFGPV
     ILFGQGGIAV EVLDDHAVGL PPLNSVLAGD MIARTRVARL LAGYRNRPAA DLEAINRTLI
     QISSLVEDLP ELVELDINPL LADGHGVIAL DARMRVAKPR STSRLAIRPY PQSLEQVTDW
     HGEALTIRPI KPEDGEAHVI FFNQLSAGDV RYRAFSSIRQ LQEPQVARLT QIDYDREMAF
     IATRVGADGQ RETLGVARAV ADADNHEAEF AIIVRSDMKG RGLGRLLMQR LIDYCRSRGT
     HFIIGETMSD NKGLLTLTQK LGFIASPIPE EHIMSLRLDL G
//
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