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Database: UniProt
Entry: G7Z3W4_AZOL4
LinkDB: G7Z3W4_AZOL4
Original site: G7Z3W4_AZOL4 
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};
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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
//
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