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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
 
 
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