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Database: UniProt
Entry: H0C0W8_9BURK
LinkDB: H0C0W8_9BURK
Original site: H0C0W8_9BURK 
ID   H0C0W8_9BURK            Unreviewed;       548 AA.
AC   H0C0W8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:EHL21623.1};
GN   ORFNames=KYG_16567 {ECO:0000313|EMBL:EHL21623.1};
OS   Acidovorax sp. NO-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL21623.1, ECO:0000313|Proteomes:UP000003485};
RN   [1] {ECO:0000313|EMBL:EHL21623.1, ECO:0000313|Proteomes:UP000003485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NO-1 {ECO:0000313|EMBL:EHL21623.1,
RC   ECO:0000313|Proteomes:UP000003485};
RX   PubMed=22374962; DOI=10.1128/JB.06814-11;
RA   Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT   "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT   Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL   J. Bacteriol. 194:1635-1636(2012).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; AGTS01000100; EHL21623.1; -; Genomic_DNA.
DR   RefSeq; WP_008905970.1; NZ_AGTS01000100.1.
DR   AlphaFoldDB; H0C0W8; -.
DR   STRING; 512030.KYG_16567; -.
DR   PATRIC; fig|512030.4.peg.3264; -.
DR   OrthoDB; 9766486at2; -.
DR   Proteomes; UP000003485; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd12118; ttLC_FACS_AEE21_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43859; ACYL-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR43859:SF4; BUTANOATE--COA LIGASE AAE1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:EHL21623.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003485}.
FT   DOMAIN          26..406
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          456..530
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   548 AA;  59172 MW;  13BC1A0128BFD70E CRC64;
     MTSIFDQHLP RNEANFAALS PLSFIERTAE VYPDRLAIVH GELRQTWAQT YARCRQLASA
     LTKAGIGKND TVAVMLPNTP PMVEAHFGVP MAGAVLNTLN TRLDPEAIAF MLDHGEAKAV
     IVDPEFSGTL AKALALRTAP TPLRVIEVQD ALYGPAVQSL GGTDYDAFVA SGDAAFAWSL
     PADEWDAIAL NYTSGTTGNP KGVVYHHRGA ATNAISNVLE WDMPKHAVYL WTLPMFHCNG
     WCFPWTIAAR AGVNVCLRRV DAQAIFDAIR NHGVTHYCGA PIVHGLLVNA PDAMKAGIPA
     GVKAMVAGAA PPASMIEGME KMGFDLTHVY GLTEVYGPAT VCAKHEAWDG LDIGERARLN
     ARQGVRYHLE RDVRVLDPET MLPVPQDGET MGEIMFKGNI AMKGYLKNPK ATEEAFAGGW
     FHSGDLAVQY PDGYIKIKDR SKDIIISGGE NISSIEVEDV LYRHPDVLAA AVVAKPDAKW
     GETPCAFVEL KAGAQTTPED IVAHCKKHLA GFKVPRAVVF GELPKTSTGK IQKFELRKQA
     GSAAAIDL
//
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