ID G7Z3W4_AZOL4 Unreviewed; 374 AA.
AC G7Z3W4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Dihydrolipoyllysine-residue acetyltransferase {ECO:0000313|EMBL:CBS86093.1};
DE EC=2.3.1.12 {ECO:0000313|EMBL:CBS86093.1};
GN Name=acoC {ECO:0000313|EMBL:CBS86093.1};
GN OrderedLocusNames=AZOLI_0734 {ECO:0000313|EMBL:CBS86093.1};
OS Azospirillum lipoferum (strain 4B).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS86093.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ311868; CBS86093.1; -; Genomic_DNA.
DR AlphaFoldDB; G7Z3W4; -.
DR STRING; 862719.AZOLI_0734; -.
DR KEGG; ali:AZOLI_0734; -.
DR HOGENOM; CLU_020336_13_2_5; -.
DR OMA; HCIHHDA; -.
DR Proteomes; UP000005667; Chromosome.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR46438; ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR46438:SF11; LIPASE-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:CBS86093.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Transferase {ECO:0000313|EMBL:CBS86093.1}.
FT DOMAIN 6..81
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 374 AA; 39282 MW; 951C55860BDD81E3 CRC64;
MLNERIKPIV MPKWGLSMSE GKVTGWLKRP GSTISIGDEL LEVETDKITN VVEAGETGVL
RRVLGEPGTV YPVKALIAVL AEPDVPDDDI DAFISAYAVP ASEDDGEADA GPQYHTAETP
AGTIRYAKRG ETGPTVLLVH GFGGDLDNWL FTIDALAESA TVYALDLPGH GQSTKQIADP
SLSGLSQAVL GFLDSVGVER AHFVGHSMGG AVSMRTALDA PGRVASLSLI ASAGLGEQID
NGYIQGFVGA TSRRDLKPVL ETLFADRGLV SRQMVDDLLK YKRLDGVDEA LRALSASLFS
DGRQASVLAS GIADARTPTL VVWGEEDRVI PADHAQALAN TAQVAVIPGA GHMVQMEAAG
KVNALLKGHI AKAD
//