ID   SAFD_NEPCE              Reviewed;         456 AA.
AC   Q2BN77;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Sulfoacetaldehyde dehydrogenase;
DE            EC=1.2.1.73;
GN   Name=safD; ORFNames=MED92_03203;
OS   Neptuniibacter caesariensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Neptuniibacter.
OX   NCBI_TaxID=207954;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED92;
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-8, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=MED92;
RX   PubMed=18506422; DOI=10.1007/s00203-008-0386-2;
RA   Krejcik Z., Denger K., Weinitschke S., Hollemeyer K., Paces V., Cook A.M.,
RA   Smits T.H.;
RT   "Sulfoacetate released during the assimilation of taurine-nitrogen by
RT   Neptuniibacter caesariensis: purification of sulfoacetaldehyde
RT   dehydrogenase.";
RL   Arch. Microbiol. 190:159-168(2008).
CC   -!- FUNCTION: Mediates conversion of 2-sulfoacetaldehyde into sulfoacetate.
CC       The enzyme is specific for NAD; NADP is not a substrate. Part of a
CC       pathway that can utilize the amino group of taurine as a sole source of
CC       nitrogen for growth. {ECO:0000269|PubMed:18506422}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + sulfoacetaldehyde = 2 H(+) + NADH +
CC         sulfoacetate; Xref=Rhea:RHEA:25637, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58246, ChEBI:CHEBI:58824; EC=1.2.1.73;
CC         Evidence={ECO:0000269|PubMed:18506422};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.12 mM for 2-sulfoacetaldehyde {ECO:0000269|PubMed:18506422};
CC         KM=0.49 mM for NAD {ECO:0000269|PubMed:18506422};
CC       pH dependence:
CC         Optimum pH is 9.0. {ECO:0000269|PubMed:18506422};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18506422}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AAOW01000005; EAR61922.1; -; Genomic_DNA.
DR   RefSeq; WP_007022657.1; NZ_CH724127.1.
DR   AlphaFoldDB; Q2BN77; -.
DR   SMR; Q2BN77; -.
DR   STRING; 207954.MED92_03203; -.
DR   KEGG; ag:EAR61922; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OMA; ALRWCGT; -.
DR   OrthoDB; 384611at2; -.
DR   BioCyc; MetaCyc:MON-14089; -.
DR   Proteomes; UP000002171; Unassembled WGS sequence.
DR   GO; GO:0102984; F:sulfoacetaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd07146; ALDH_PhpJ; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR017656; Put_phosphonoacetaldehyde_DH.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:18506422"
FT   CHAIN           2..456
FT                   /note="Sulfoacetaldehyde dehydrogenase"
FT                   /id="PRO_0000418499"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000250"
FT   BINDING         213..218
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  49258 MW;  91551119B922F4C8 CRC64;
     MSNTYSLVNP FDNSPLGEYE YTPWATLENQ LAMLKEGQLS QRKTAAFQRA GVLNKLAALL
     KEHSEEMATL ITQETGKTIL DSRVEMMRAY NAAIASAEEA RQIQGESLDS DAYAPAGGKI
     GVVCWKPLGT ILCITPFNFP INIAIHKIGP AYAAGNTILF KPGPQNTASA QLLVKLCYEA
     GMPENTLQLC MPEFSDLDRL NAHPDVNAIN FTGGTAAANA ISAAAGYKKL LLELGGNDPL
     IVMDDGDLEA ATTAAINHRF ATAGQRCTAA KRLFIHANVY EAFRDLLVEK SSKLVVGDPM
     KDDTFVGPVI NQGAADQIRT LIEQAIEDGA SVALGNQYEG AFVYPTILEN VSPTSEIMVE
     EAFGPVMPLY KFESVEEIIP IINNTAYGLQ AGVFSQNLAT IKELYEQLDV GTLAANDGPG
     FRTEHFPFGG VKESGIGREG IKYAIREMSY TKTLVI