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Database: UniProt/TrEMBL
Entry: S6ALT0_PSERE
LinkDB: S6ALT0_PSERE
Original site: S6ALT0_PSERE 
ID   S6ALT0_PSERE            Unreviewed;       310 AA.
AC   S6ALT0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:BAN46368.1};
GN   ORFNames=PCA10_06360 {ECO:0000313|EMBL:BAN46368.1};
OS   Pseudomonas resinovorans NBRC 106553.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN46368.1, ECO:0000313|Proteomes:UP000015503};
RN   [1] {ECO:0000313|EMBL:BAN46368.1, ECO:0000313|Proteomes:UP000015503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN46368.1,
RC   ECO:0000313|Proteomes:UP000015503};
RX   PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA   Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA   Fujita N., Nojiri H.;
RT   "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT   resinovorans Strain CA10 (NBRC 106553).";
RL   Genome Announc. 1:e00488-13(2013).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; AP013068; BAN46368.1; -; Genomic_DNA.
DR   RefSeq; WP_016490570.1; NC_021499.1.
DR   AlphaFoldDB; S6ALT0; -.
DR   STRING; 1245471.PCA10_06360; -.
DR   KEGG; pre:PCA10_06360; -.
DR   PATRIC; fig|1245471.3.peg.642; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_2_6; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000015503; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd12156; HPPR; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015503}.
FT   DOMAIN          42..309
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          106..278
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   310 AA;  33393 MW;  010083762C15AD15 CRC64;
     MKILHIGPLT ERFNQRLVTE NDVVQLWRQG DALAYLDAHG GEFDIVVTSA RFGCSAAMLE
     RLPKVRAICS FGVGYDAIAV DVARDRGIRV SSTPDVLNDC VADLAMGLVI DCSRRISASD
     RFVRAGLWPA GNFPLARKVS GKRLGIVGLG RIGKDVARRA GGFDMQVRYH NRRPDADAPY
     GYEPDLLALA RWADFLVLLC PGGAATHHLI SAPVLDALGP EGILVNVARG SVVDEQALVA
     ALVEGRLGGA ALDVFEAEPQ VPEVLYGLDN VVLTPHIGSG TEETRLQMEE LVFANLRAFL
     DTGEMLTPVV
//
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