ID Q1YNA3_AURMS Unreviewed; 897 AA.
AC Q1YNA3;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Acetyltransferase, GNAT family {ECO:0000313|EMBL:EAS51128.1};
GN ORFNames=SI859A1_01939 {ECO:0000313|EMBL:EAS51128.1};
OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Aurantimonadaceae; Aurantimonas.
OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS51128.1, ECO:0000313|Proteomes:UP000000321};
RN [1] {ECO:0000313|EMBL:EAS51128.1, ECO:0000313|Proteomes:UP000000321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS51128.1,
RC ECO:0000313|Proteomes:UP000000321};
RX PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT Aurantimonas sp. strain SI85-9A1.";
RL Appl. Environ. Microbiol. 74:2646-2658(2008).
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:EAS51128.1}.
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DR EMBL; AAPJ01000001; EAS51128.1; -; Genomic_DNA.
DR RefSeq; WP_009209772.1; NZ_CH672387.1.
DR AlphaFoldDB; Q1YNA3; -.
DR HOGENOM; CLU_007415_0_2_5; -.
DR OrthoDB; 9807426at2; -.
DR BioCyc; AURANTIMONAS:SI859A1_01939-MONOMER; -.
DR Proteomes; UP000000321; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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; 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; 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:UP000000321};
KW Transferase {ECO:0000313|EMBL:EAS51128.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 496..549
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 734..894
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 897 AA; 95918 MW; 525583CA1DE1C1B9 CRC64;
MSIRNFDALF APRSIALIGA SNEPGSVGSV LVDNLVSGGF AGRIMLVNPH AREIHGRQCH
RSVETLPEVP DLAVIATPAR TVPGIISALG ERGCCAAIVI SAGLGEAVDG ATLRQQVLDA
ARPHLMRIVG PNCLGLISPA AGINASFAHL MPRAGDIALV SQSGAMLTSV IDWADERRIG
FSHLLSVGDM SDVDFGDMLD YLATDRTTRS ILLYVENVTE AQKFLSAARL AARSMPVLVI
KAGRSAAGAR AAQSHTGALA GSDVVYDAAF RRAGILRVRE IEELFEAAAT LASGVRISGD
RLTILTNGGG AGVLAVDALE SDGGRLARLS EEGIAALDGV LPPTWSRANP VDIIGDATPE
RYGAALDILM KERESDAILV INCPTAVADG MEAGRRIAAI AKRRPRFPVL TNWLGGTSAA
PVRDLFAAEK VATFDSPEKA IRAFTHLVEY KRNQELLLET PSAGVAIGHE DIASAQELIE
TVRRDGRTIL SEYEAKRLLA TFGIPTVTTR MAGDVDGAVA CFEAIGAPAV LKIVSAEISH
KSDAGGVRLN IGSAQEMRES AEAMLEAVRA YAPHARIDGF TVQPMIVRDG AYELIAGIAP
DPTFGPVILF GRGGKAAEVI GDRAIGLPPL NSVLAREMIR ATRISKLLAG YRDVAPVAFD
ALADVLVRLS ELAVHLPDVA ELDINPLLAD AEGVLALDAR ISLHAAGAVR VAPSIRPYPR
ELERAVELRN GERFVLRPIR PEDEDPLVEM VARCTQEDLR LRFMAPMKAL PHQTAARFSQ
IDYHREMALV AVEPGSAYGQ GPIYGVARLV SDPENEAAEF AVLVRSDMKG RGLGYRLLSE
ILAYGRKRGL HRVYGEVLRE NVTMLQMARD LGFRADRTED FSETAHVTIE FDREADA
//
