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Database: UniProt
Entry: A0A1R1I7V8_9RHOO
LinkDB: A0A1R1I7V8_9RHOO
Original site: A0A1R1I7V8_9RHOO 
ID   A0A1R1I7V8_9RHOO        Unreviewed;       898 AA.
AC   A0A1R1I7V8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=GNAT family N-acetyltransferase {ECO:0000313|EMBL:OMG54795.1};
GN   ORFNames=BJN45_06335 {ECO:0000313|EMBL:OMG54795.1};
OS   Azonexus hydrophilus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Azonexus.
OX   NCBI_TaxID=418702 {ECO:0000313|EMBL:OMG54795.1, ECO:0000313|Proteomes:UP000187526};
RN   [1] {ECO:0000313|EMBL:OMG54795.1, ECO:0000313|Proteomes:UP000187526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS02 {ECO:0000313|EMBL:OMG54795.1,
RC   ECO:0000313|Proteomes:UP000187526};
RA   Salah Z., Rout S.P., Humphreys P.N.;
RT   "Alkaliphiles isolated from bioreactors.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OMG54795.1}.
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DR   EMBL; MTHD01000002; OMG54795.1; -; Genomic_DNA.
DR   RefSeq; WP_076093188.1; NZ_MTHD01000002.1.
DR   AlphaFoldDB; A0A1R1I7V8; -.
DR   STRING; 418702.BJN45_06335; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000187526; 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   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; 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; PF13302; Acetyltransf_3; 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:UP000187526};
KW   Transferase {ECO:0000313|EMBL:OMG54795.1}.
FT   DOMAIN          497..533
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          739..897
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   898 AA;  98487 MW;  4C0DAE773E66FFA1 CRC64;
     MLEQHYLTAL FEPKSVAVIG ASDRENSVGN IIFKNILGSG YKGRLYAINP KHETIQGQPA
     YKSIEEIGAR VEMAVIATRP QTVPQIIEQC GRSGVRNVIV IASGFSEAGH IGAALERKVM
     EIARSYNVRV LGPNCLGIIR PELGLNATFT KITADPGNLA LVSQSGAMCS AVLDWAKANQ
     VGFSSVISLG MTADVDFGEI LDYLIYDSRT HYILMYVEGI RNARRFMSAL RSAARIKPII
     LLKAGRHEAG SQAATAHSGM AAISDTVFDA AVRRAGVVRV KNVGQLFYAA KALASKFRPQ
     GDRLAIITNG GGPGAMAADR AGDLGIPLAQ LSTETMGNLN KVLPTNWSHS NPVDIGGDAT
     PERYRDALLS ISQDPNVDST LVMLSPQAMT DPLGVAQAII SISDKLNRRI ICCWMGEAQV
     AEARKLLEDS GIPAFRMPET AIELFHHISK YYRNQKLLLQ TPEPTRQHGR PETEGAKMLI
     EALLAERRKV LSEMESKAIL RAFKVPVAQT MVARTATEAL LLAEQIGFPV AMKVDSPELP
     HKSDAGGVRL NIQNAPAVRN AYHDIIDTVQ KRHPTAKING VSIEPFLSRP HGREIMIGVI
     RDPIFGPVIT FGAGGFDNEI FSDRSVALPP LNKFLAKDLI ESTRTSKILD QFHNMPPVDR
     EAIKEVLLCI SEMVCELPWI IELDINPLIV DEHGAIAADA RIVIDHAANS SGDRYAHMAI
     YPYPVHLIQD WTMNDGKVVT IRPIRPEDAD MEQEFVKAMS DESRYYRFMD TLRELTQTML
     VRFTQIDYDR EMALVATLPD PESGKESQIG VARYVLNPDG ESVEFALAVG DDWQKCGVGR
     KLMTALIDCA RMKGYRAVVG DVLSTNSKMF RLMTSLGFTI HPHPDDTAVK RVVKPLTG
//
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