ID   SAUT_CUPNH              Reviewed;         509 AA.
AC   Q0K844;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Probable sulfoacetate--CoA ligase;
DE            EC=6.2.1.-;
GN   Name=sauT; OrderedLocusNames=H16_A2748;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND GENE
RP   NAME.
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=20693281; DOI=10.1074/jbc.m110.127043;
RA   Weinitschke S., Hollemeyer K., Kusian B., Bowien B., Smits T.H., Cook A.M.;
RT   "Sulfoacetate is degraded via a novel pathway involving sulfoacetyl-CoA and
RT   sulfoacetaldehyde in Cupriavidus necator H16.";
RL   J. Biol. Chem. 285:35249-35254(2010).
CC   -!- FUNCTION: Catalyzes the CoA- and ATP-dependent conversion of
CC       sulfoacetate to sulfoacetyl-CoA and AMP. {ECO:0000269|PubMed:20693281}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20693281}.
CC   -!- INDUCTION: Induced by sulfoacetate. {ECO:0000269|PubMed:20693281}.
CC   -!- DISRUPTION PHENOTYPE: Mutants do not grow with sulfoacetate, but can
CC       use acetate, taurine, isethionate and sulfoacetaldehyde.
CC       {ECO:0000269|PubMed:20693281}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AM260479; CAJ93827.1; -; Genomic_DNA.
DR   RefSeq; WP_011615810.1; NZ_CP039287.1.
DR   AlphaFoldDB; Q0K844; -.
DR   SMR; Q0K844; -.
DR   STRING; 381666.H16_A2748; -.
DR   EnsemblBacteria; CAJ93827; CAJ93827; H16_A2748.
DR   GeneID; 57644872; -.
DR   KEGG; reh:H16_A2748; -.
DR   PATRIC; fig|381666.6.peg.3144; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_10_4; -.
DR   OMA; VPTMWIA; -.
DR   OrthoDB; 961884at2; -.
DR   BioCyc; MetaCyc:MON-15851; -.
DR   Proteomes; UP000008210; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd05926; FACL_fum10p_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 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.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR045310; Pcs60-like.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..509
FT                   /note="Probable sulfoacetate--CoA ligase"
FT                   /id="PRO_0000418823"
FT   REGION          320..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   509 AA;  54259 MW;  E199FE029A11E0A3 CRC64;
     MNARTEPEVF DTLAALIAVR AAQWPDKPYL LSPDSGHALT FGALATDAGT LGRSYAAAGL
     GSGQTVSVYL PNGEQTARLL LGTMACGLVV NPINLLCQPA QLRYILAHSD TRLVFTWPDG
     EAAIREALRE AGLDVPVLVT APDANSLPAL PATHDAASPL PPPQPDAPAL LMYTSGTTGT
     PKGVLLTQRN LVANGTNVSR EHCLGPADRV LATLPLYHIN GLVVTAIAPL VHGGSVVMPM
     RFSASAFWQD SARHGCTWLN VVPTIIAYLL NDPHGQAPAG VRFCRSASAA LPPEHHRAFE
     ARFGIGVIET MGMTETAAPA FSNPLDPGQR RIGSIGRPSG TRARVLGRDG KPAPDGQVGE
     IVLQGESVMA GYYKAPDITR EAFTHDGWLR TGDLGYRDAD GYFYISGRAK ELIIKGGENI
     APREIDEALL RHPGVLEAAA VGVPDPAYGQ EIVAYVVMRE AARCDDAALR AHCLRELGRY
     KTPKEFRFIA ELPRGPSGKV QRLKLLNHA