ID A1B2J5_PARDP Unreviewed; 593 AA.
AC A1B2J5;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN OrderedLocusNames=Pden_1642 {ECO:0000313|EMBL:ABL69739.1}, Pden_4277
GN {ECO:0000313|EMBL:ABL72341.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL69739.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|EMBL:ABL69739.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PD1222 {ECO:0000313|EMBL:ABL69739.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of Chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABL72341.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PD1222 {ECO:0000313|EMBL:ABL72341.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of Chromosome 2 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000489; ABL69739.1; -; Genomic_DNA.
DR EMBL; CP000490; ABL72341.1; -; Genomic_DNA.
DR RefSeq; WP_011747937.1; NC_008687.1.
DR AlphaFoldDB; A1B2J5; -.
DR STRING; 318586.Pden_1642; -.
DR EnsemblBacteria; ABL69739; ABL69739; Pden_1642.
DR EnsemblBacteria; ABL72341; ABL72341; Pden_4277.
DR GeneID; 75503659; -.
DR KEGG; pde:Pden_1642; -.
DR KEGG; pde:Pden_4277; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000000361; Chromosome 1.
DR Proteomes; UP000000361; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050487; F:sulfoacetaldehyde acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019529; P:taurine catabolic process; IEA:InterPro.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR017820; Sulphoacetald_Actrfrase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR03457; sulphoacet_xsc; 1.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:ABL69739.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABL69739.1}.
FT DOMAIN 3..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 187..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 404..557
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 593 AA; 64363 MW; 603FF89FF307096E CRC64;
MKMTTEESFV KTLQLHGIEH AFGIIGSAMM PVSDLFPRAG ITFWDCAHET NAGMMADGFT
RSTGRMSMAI AQNGPGVTGF VTPVKTAYWN HTPLLLVTPQ AANRTIGQGG FQEMEQMRIF
ADCVCYQEEV RDPSRIPEVL NRVIMQAWRN SAPAQINIPR DFWTQVIDVD LPQVVGFERP
AGGERAVAEA ARLLSEARFP VILSGAGVVL SGAIPDLVGL AERLDAPVCS NYQHNDSFPG
SHPLAMGPLG YNGSKAAMEI IARADVVLAL GTRLNPFSTL PGYGIDYWPK DARIIQVDIN
ADRIGLTKKV AVGIQGDAAK VARGILAQLA PAAGDAGRQE RRDLVAQTRS RWAQELSSLD
HEEDDPGTEW NEQARARDAG LMSPRQAWRA IMQAVPKEAI VSSDIGNNCA IGNAYPSFEA
GRKYLAPGLF GPCGYGFPAI LGAKIGNPEV PVIGFAGDGA FGISMNEMTA CGREDWPAIT
MVIFRNYQWG AEKRNTTLWY DNNFVGTELD RDTSYAKIAQ ACGLVGVQVR SQEELTAALH
DAVERQMQGR ETTFIEVLLN QELGEPFRRD AMKKPVAVAG IDPADMRPQQ GAA
//
