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Database: UniProt/TrEMBL
Entry: K4KZS6_9FIRM
LinkDB: K4KZS6_9FIRM
Original site: K4KZS6_9FIRM 
ID   K4KZS6_9FIRM            Unreviewed;       560 AA.
AC   K4KZS6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Acyl-coenzyme A synthetase/AMP-(Fatty) acid ligase {ECO:0000313|EMBL:AFV04740.1};
GN   ORFNames=DCF50_p733 {ECO:0000313|EMBL:AFV04740.1};
OS   Dehalobacter sp. CF.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Dehalobacter.
OX   NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV04740.1, ECO:0000313|Proteomes:UP000000482};
RN   [1] {ECO:0000313|EMBL:AFV04740.1, ECO:0000313|Proteomes:UP000000482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF {ECO:0000313|EMBL:AFV04740.1};
RX   PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA   Tang S., Gong Y., Edwards E.A.;
RT   "Semi-automatic in silico gap closure enabled de novo assembly of two
RT   dehalobacter genomes from metagenomic data.";
RL   PLoS ONE 7:E52038-E52038(2012).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP003870; AFV04740.1; -; Genomic_DNA.
DR   RefSeq; WP_015042744.1; NC_018867.1.
DR   AlphaFoldDB; K4KZS6; -.
DR   STRING; 1131462.DCF50_p733; -.
DR   KEGG; dec:DCF50_p733; -.
DR   PATRIC; fig|1131462.4.peg.743; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_59_10_9; -.
DR   Proteomes; UP000000482; Chromosome.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
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; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR   PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 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:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AFV04740.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000482}.
FT   DOMAIN          43..413
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          464..542
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   560 AA;  63200 MW;  79440E2C2EAA9F9E CRC64;
     MNLASRYIGK TDFDSYEDFC ANYQVKVPDN FNFAYDIVDE YGRLEPERPA LVWCDDHGNE
     RIFTFADLKK YSDKTANMLS EAGIRKGDKV MLILRRRYEV YIAILALAKI GAIYIPSSNQ
     LTQKDIIYRN NAASIKAIIA YHDPVILDHV EASREESSTL ETLFLVGARR PGWVDFDSSM
     EAASENWVRP TGADATTNDD TMIIYFTSGT TSMPKMAIQS FTYPLGHIVT AKYWQRVVDG
     GLHLTVSDSG WAKFGWGKIY GQWICGAVQF VYDMDKFIPE KLLEMMQKYK LSTFCAPPTI
     YRFLLEHNLE KYNLSSIVHC STAGEPLNPD VFNRFKSITG LSILNGFGQS ETTVLVANFE
     WLDIYPGAMG KPNPAYKIDV VDENGAPCPP GVEGELVIRE ADSNKPAGLF CGYYMDETAT
     NKVWYDDTYH TGDMAYWDEH GFLWFVGRND DVIKASGYRI SPFEVESALI EHPAVVECAV
     TGAPDAVRGT VVKATVVLAK GYTASELLKK EIQDYVKKVT APYKYPRILE FVDELPKTIG
     GKIKRAQIRR EDTEKFQDKE
//
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