ID V4YT78_9PROT Unreviewed; 600 AA.
AC V4YT78;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:ESS14867.1};
GN ORFNames=MOLA814_00433 {ECO:0000313|EMBL:ESS14867.1};
OS Betaproteobacteria bacterium MOLA814.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1408164 {ECO:0000313|EMBL:ESS14867.1, ECO:0000313|Proteomes:UP000017838};
RN [1] {ECO:0000313|EMBL:ESS14867.1, ECO:0000313|Proteomes:UP000017838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOLA814 {ECO:0000313|EMBL:ESS14867.1,
RC ECO:0000313|Proteomes:UP000017838};
RX PubMed=24356832;
RA Courties A., Riedel T., Jarek M., Intertaglia L., Lebaron P., Suzuki M.T.;
RT "Genome Sequence of Strain MOLA814, a Proteorhodopsin-Containing
RT Representative of the Betaproteobacteria Common in the Ocean.";
RL Genome Announc. 1:e01062-13(2013).
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:ESS14867.1}.
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DR EMBL; AYMW01000001; ESS14867.1; -; Genomic_DNA.
DR AlphaFoldDB; V4YT78; -.
DR STRING; 1408164.MOLA814_00433; -.
DR PATRIC; fig|1408164.3.peg.758; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000017838; 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:SF169; 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 ECO:0000313|EMBL:ESS14867.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017838};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:ESS14867.1}.
FT DOMAIN 13..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 420..571
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 600 AA; 64928 MW; 5400CBDC31BF8AE6 CRC64;
MSSTTVTSGP QRMTPSEAFV ETMVARGVKT MFGIMGSAFM DAMDIFAPAG ITLIPVVHEQ
GAGHMADGYA RVTGRHGVVI GQNGPGISNC VTSIAAAFWA HSPVVMITPE TGTMGMGLGG
FQEANQLPMF QEFTKYQGHV NNPKRMAEYT ARCFDRAISE MGPTQLNIPR DHFYGEITCE
IPAEQVIERG HGGENSLNAA AELLATAKFP VILAGGGVVM GNAVAECQAL AERLGAPVVT
GYLRNDAFPA SHPLWAGPLG YQGSKAAMKL IAQADVVIAL GSRMGPFGTL PQHGMDYWPK
DAKIIQVEAD HTNLGLVKKI SVGVCGDAKA AAKAIYERLN NKTLACDSTK EARAKTIASE
KAAWEKELDE WTHERDTFSL DMIEEAKGET PFSGGEYLHP RQVLRELEKA MPKRVMVSTD
IGNINSVANS YLRFDEPRSF FAPMSFGNCG YALPTIIGAK VAAPERPAVA YAGDGAWAMS
MVEIMTAVRH NIPVTAVVFH NRQWGAEKKN QVDFYNRRFV AGELESESFA GMATAMGAEA
IIVDKLEDVG TALKKAIDMQ MNEGKTCVIE IMCTRELGDP FRRDALAKPV RLLDKYKDFV
//