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Database: UniProt
Entry: A0A225NNW1_9RHOB
LinkDB: A0A225NNW1_9RHOB
Original site: A0A225NNW1_9RHOB 
ID   A0A225NNW1_9RHOB        Unreviewed;       591 AA.
AC   A0A225NNW1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=sulfoacetaldehyde acetyltransferase {ECO:0000256|ARBA:ARBA00012971};
DE            EC=2.3.3.15 {ECO:0000256|ARBA:ARBA00012971};
GN   ORFNames=ATO3_07755 {ECO:0000313|EMBL:OWU76053.1};
OS   Marinibacterium profundimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Marinibacterium.
OX   NCBI_TaxID=1679460 {ECO:0000313|EMBL:OWU76053.1, ECO:0000313|Proteomes:UP000215377};
RN   [1] {ECO:0000313|EMBL:OWU76053.1, ECO:0000313|Proteomes:UP000215377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II1-22F33 {ECO:0000313|EMBL:OWU76053.1,
RC   ECO:0000313|Proteomes:UP000215377};
RA   Lai Q., Li G., Shao Z.;
RT   "Oceanicola sp. 22II1-22F33 Genome Sequencing.";
RL   Submitted (APR-2013) 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:OWU76053.1}.
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DR   EMBL; AQQR01000002; OWU76053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A225NNW1; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000215377; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000215377};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OWU76053.1}.
FT   DOMAIN          3..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          404..556
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   591 AA;  63722 MW;  BAD6623AC921249C CRC64;
     MKMTTEEAFV KTLQRHGIEH AFGIIGSAFM PISDLFPKAG ITFWDCAHEG SGGMMADGYT
     RATGKMSMMI AQNGPGITNF VTAVKTAYWN HSPLLLVTPQ AANKTLGQGG FQEVEQMALF
     KDMVAYQEEV RDPSRVAEVL NRVIIQAKRA SAPAQINMPR DFWTQVIDIE IPEVLEFERP
     GGGETALDAA AALLSEAKFP VILNGAGVVL ANAIPESMAL AEQLDAPVCV GYQHNDAFPG
     SHPLFAGPLG YNGSKAGMEL IAQADVVLCL GTRLNPFSTL PGYGMEYWPK GAKIIQVDIN
     PDRIGLTKPV SVGIVGDARK VAGALLSRLS DSAGDTGREA RKAVIAETKS RWAQQLSSMD
     HEEDDPGTTW NERARADKPE WMSPRMAWRA IQSALPREAI ISSDIGNNCA IGNAYPSFEA
     GRKYLAPGLF GPCGYGLPSI VGAKIGCPDV PVVGFAGDGA FGIAVTELTA IGRKEWPAIT
     MVVFRNYQWG AEKRNSTLWY DDNFVGTELD DDVTYAGIAK ACGLQGIVAR TMEGLTEALT
     TAIRDQMEHG RTTLIEALIN QELGEPFRRD AMKKPVAVAG IDPADMRRQV V
//
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