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Database: UniProt
Entry: V4YT78_9PROT
LinkDB: V4YT78_9PROT
Original site: V4YT78_9PROT 
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
//
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