ID A4J977_DESRM Unreviewed; 211 AA.
AC A4J977;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Transferase hexapeptide repeat containing protein {ECO:0000313|EMBL:ABO51630.1};
GN OrderedLocusNames=Dred_3128 {ECO:0000313|EMBL:ABO51630.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO51630.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO51630.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO51630.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000612; ABO51630.1; -; Genomic_DNA.
DR RefSeq; WP_011879418.1; NC_009253.1.
DR AlphaFoldDB; A4J977; -.
DR STRING; 349161.Dred_3128; -.
DR KEGG; drm:Dred_3128; -.
DR eggNOG; COG0110; Bacteria.
DR HOGENOM; CLU_081811_2_0_9; -.
DR OrthoDB; 9801456at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd03360; LbH_AT_putative; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR020019; AcTrfase_PglD-like.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR041561; PglD_N.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR03570; NeuD_NnaD; 1.
DR PANTHER; PTHR43300; ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43300:SF7; UDP-N-ACETYLBACILLOSAMINE N-ACETYLTRANSFERASE; 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF17836; PglD_N; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABO51630.1}.
FT DOMAIN 6..74
FT /note="PglD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17836"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR620019-1"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR620019-2"
FT BINDING 143
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|PIRSR:PIRSR620019-2"
FT SITE 135
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|PIRSR:PIRSR620019-1"
SQ SEQUENCE 211 AA; 22086 MW; 59ACAE9E4161E68C CRC64;
MKTLSLLIMG CGGHARSVAD IALHIGFKEL LFVDHGARPG EQIFSFDVHK TFPTSLPMGC
LVFPASGDNW QRMHQIQIAI ENGFSLTNIV SPLAYLGAGV TVGEGTLLAH HAHVGPSAII
GKGGIINTGA VVEHECQIGD FSHISVNATI AGRCKIGKRV FIGAGAIVID KVRIADDVVI
GAGATVVEDL IESGVYVGTP ASLVKNKSHV F
//
