ID A0A257EIP6_9BURK Unreviewed; 606 AA.
AC A0A257EIP6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN Name=xsc {ECO:0000313|EMBL:OYU13371.1};
GN ORFNames=CFE38_03720 {ECO:0000313|EMBL:OYU13371.1};
OS Comamonadaceae bacterium PBBC1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=2015580 {ECO:0000313|EMBL:OYU13371.1, ECO:0000313|Proteomes:UP000216161};
RN [1] {ECO:0000313|EMBL:OYU13371.1, ECO:0000313|Proteomes:UP000216161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBBC1 {ECO:0000313|EMBL:OYU13371.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYU13371.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NKIP01000002; OYU13371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257EIP6; -.
DR Proteomes; UP000216161; Unassembled WGS sequence.
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 CDD; cd02013; TPP_Xsc_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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR03457; sulphoacet_xsc; 1.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:OYU13371.1}.
FT DOMAIN 19..133
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..339
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 426..577
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 606 AA; 65816 MW; B56E9CC8F6B4E53D CRC64;
MTTPQKTDKR TVASGVQKMT PSEAFVETMV ANGVTDMFGI MGSAFMDAMD IFAPAGIRLI
PVVHEQGGAH MADGYARVSG RHGVVIGQNG PGISNCVTAI AAAYWAHSPV VIVTPETGTM
GMGLGGFQEA QQLPMFQEFT KYQGHVNNPK RMAEFTARCF DRAISEMGPT QLNIPRDYFY
GEVNCEIPQP MRVERGAGGE NSLNAAVELL ANAKFPVILS GGGVVMGDAV KECVALAERL
GSPVANGYLR NDSFPASHPL WAGPLGYQGS KAAMKLIAQA DVVVALGSRM GPFGTLPQHG
MDYWPKEAKI IQVEADHTNL GLVKKITVGI HGDAKAVAIE LLKRLSARTL ACDANKAERA
AKIQAEKDAW EKELDAWTHE KDPFSLDMME EAKGERTPTG GTYLSPRQVL RELEKAMPPR
VMVSTDIGNI NAVANSYLRF DEPRSFFAPM SFGNCGYSLP TMIGAKCAAP DRPAVAYAGD
GAWGMSMVEV MTAVRHDIPV TAVVFHNRQW GAEKKNQVDF YNRRFVAGEL ESESFAGIAQ
AMGAEGIVVD RLEDVGPALK KAIDLQMNQR KTCVIEIMCN RELGDPFRRD ALAKPIRFLD
KYKDYV
//
