AT_OCEGH
ID AT_OCEGH Reviewed; 206 AA.
AC Q2CEE2;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Putative acetyltransferase OgpAT {ECO:0000303|PubMed:24088714};
DE Short=OgpAT;
DE EC=2.3.-.-;
GN ORFNames=OG2516_04134 {ECO:0000312|EMBL:EAR51055.1};
OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS HTCC2516).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=314256 {ECO:0000312|EMBL:EAR51055.1};
RN [1] {ECO:0000312|EMBL:EAR51055.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000312|EMBL:EAR51055.1};
RX PubMed=20418400; DOI=10.1128/jb.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ACETYL-COA,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF 144-GLY--GLY-146.
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000303|PubMed:24088714};
RX PubMed=24088714; DOI=10.1098/rsob.130021;
RA Rao F.V., Schuttelkopf A.W., Dorfmueller H.C., Ferenbach A.T.,
RA Navratilova I., van Aalten D.M.;
RT "Structure of a bacterial putative acetyltransferase defines the fold of
RT the human O-GlcNAcase C-terminal domain.";
RL Open Biol. 3:130021-130021(2013).
CC -!- FUNCTION: Binds acetyl-CoA, but not butyryl-CoA or decanoyl-CoA. May
CC have acetyltransferase activity. {ECO:0000269|PubMed:24088714}.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:24088714}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AAOT01000018; EAR51055.1; -; Genomic_DNA.
DR RefSeq; WP_007254355.1; NZ_CH724107.1.
DR PDB; 3ZJ0; X-ray; 1.80 A; A=1-206.
DR PDBsum; 3ZJ0; -.
DR AlphaFoldDB; Q2CEE2; -.
DR SMR; Q2CEE2; -.
DR STRING; 314256.OG2516_04134; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_086044_1_0_5; -.
DR OMA; YQRKGWG; -.
DR OrthoDB; 1972497at2; -.
DR Proteomes; UP000003635; Unassembled WGS sequence.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..206
FT /note="Putative acetyltransferase OgpAT"
FT /id="PRO_0000430933"
FT DOMAIN 5..205
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 135..138
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24088714"
FT BINDING 144..148
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24088714"
FT BINDING 175..177
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24088714"
FT BINDING 184
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24088714"
FT MUTAGEN 144..146
FT /note="GRG->DPS: Abolishes acetyl-CoA binding."
FT /evidence="ECO:0000269|PubMed:24088714"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 147..161
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3ZJ0"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:3ZJ0"
SQ SEQUENCE 206 AA; 22238 MW; DB2BF804D5528AFE CRC64;
MASEVVIRRA TAADHGDLCR VCLLTGDSGR DASSREDDPT LLGMIYAVPY QVGAPDFAFV
LEDAEGVCGY LLGAPDTLSF QHFLEKEWLP PLRAGLTDPG PDPAAWQGSD WARDAIHRPP
ALPPIDLAAY PAHGHIDLLP RAQGRGVGSR AMDHLEAALA AAGAPGMHLQ VSPENPRALG
FYEHRGFREL CRSEDEVVVG RRLLDE