ID H1G6R0_9GAMM Unreviewed; 893 AA.
AC H1G6R0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:EHQ53497.1};
GN ORFNames=ECTPHS_12545 {ECO:0000313|EMBL:EHQ53497.1};
OS Ectothiorhodospira sp. PHS-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ53497.1, ECO:0000313|Proteomes:UP000005314};
RN [1] {ECO:0000313|EMBL:EHQ53497.1, ECO:0000313|Proteomes:UP000005314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ53497.1,
RC ECO:0000313|Proteomes:UP000005314};
RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA Hoeft S., Oremland R.S., Stolz J.;
RT "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT oxidoreductases.";
RL Submitted (JAN-2012) 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:EHQ53497.1}.
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DR EMBL; AGBG01000036; EHQ53497.1; -; Genomic_DNA.
DR RefSeq; WP_008933064.1; NZ_AGBG01000036.1.
DR AlphaFoldDB; H1G6R0; -.
DR STRING; 519989.ECTPHS_12545; -.
DR PATRIC; fig|519989.5.peg.2460; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG0456; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000005314; 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: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; 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 Transferase {ECO:0000313|EMBL:EHQ53497.1}.
FT DOMAIN 737..893
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 893 AA; 97521 MW; ED15B6A9C1F8C046 CRC64;
MGPHFLSRIF NPRSVAVIGA SERTNALGTL VFANLIDAGF KGELYPVNPK HDTVQGRKAY
PDVEAIGRPV DMVVVATPAR TVPGILRHCG EHGVKGAVVL SAGFAESGRV GKRLEQEVME
IAKEYDLRLI GPNCLGIIRP NRGMNATFSK NRALPGNLAL VSQSGAICTG ILDWAESQEI
GFSAVVSMGD ASDVDFGDVL DYLALDRETR SILVYVEGVR NARRFMSGLR AAARMKPVIV
IKSGRHAEGS RAAMSHTGAL VGADDVFDAA LERAGAVRAM TIQQLFSAAR ILSSGYRIEG
NRLAIVTNAG GPGVMATDRA VELDIAMAQL SAATMESLNK ALPEQWSHGN PVDLLGDADA
KRFESALKAC LDDDGVDGTI VMLTPQAMTD PLGVAQAVTP VARKTQKPVL ACWMGDNQVR
TAREHFTKER LPHFTTPEAS VEAFAYLAAH KRNQRLLLQV PGPLSDRTRT DVQGARLIIE
SALSEGRKVL STMESKAILS AFRIPVTQTM RANTASEALV AAGTVGYPVA MKIDSPDITH
KSDVQGVRLN IASAESVRSA FQTMIEDTRR LRPDARINGV TIERMHKSTY GRELMVGVLR
DPVFGPVISF GSGGTSVEVI KDRAVALPPL NEVIIEGMIA RTKVAKLLKE FRNMPAVDDE
ALEQVLLRVS EMVCELPEIQ DMDINPLIAD ERGLAAVDAR LSVDYPPSMP DRYAHMAIHP
YPAHLVNNWQ LPDGINLTIR PIRPEDARIE QEFVRNLSPE ARYFRFMQAV HELTPHMLVR
FTQIDYDREM ALIAVREQPD GSELQIAVAR YTANPDQQSC EFGLVVADEW QGRGIGSHLM
NELMDVARSR GLRTMEGKVL TQNTNMIALM HRLGFTSRNS SEDDGIKVVS KRL
//
