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Database: UniProt
Entry: A0A495RC03_9GAMM
LinkDB: A0A495RC03_9GAMM
Original site: A0A495RC03_9GAMM 
ID   A0A495RC03_9GAMM        Unreviewed;       348 AA.
AC   A0A495RC03;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Galactitol 1-phosphate 5-dehydrogenase {ECO:0000313|EMBL:RKS84790.1};
GN   ORFNames=DES39_2006 {ECO:0000313|EMBL:RKS84790.1};
OS   Orbus hercynius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Orbales; Orbaceae; Orbus.
OX   NCBI_TaxID=593135 {ECO:0000313|EMBL:RKS84790.1, ECO:0000313|Proteomes:UP000278542};
RN   [1] {ECO:0000313|EMBL:RKS84790.1, ECO:0000313|Proteomes:UP000278542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22228 {ECO:0000313|EMBL:RKS84790.1,
RC   ECO:0000313|Proteomes:UP000278542};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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:RKS84790.1}.
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DR   EMBL; RBWY01000004; RKS84790.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495RC03; -.
DR   OrthoDB; 9773078at2; -.
DR   Proteomes; UP000278542; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08236; sugar_DH; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278542};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          25..131
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          172..302
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   348 AA;  38079 MW;  5BCB55464AAF782B CRC64;
     MKAIIVNEDS TLQTQELEMP VIENPQQIIV KIAYSGLCGS DIPRIFHHGA HFYPITLGHE
     FSGTIVEVGQ HVEHLKVGDN IASVPLLPCF KCDECHHHYY SLCKNYTFVG SRKAGGFAEY
     VVMDQKNAFK LPNNVSLLAG AFFEPLTVGM HGILLADGCQ DKNVIIVGAG TIGLLAMQCA
     KAMGASSIIV IDINQERLAL AKSLGADHVY NPSHLTAEQI LDAMNDLRFN QLVLETAGSP
     ITVKLSIDIA GPRAQLVLIG TLHQDLALPE KTFGLILRKE LTIMGSWMNY SAPWPGKEWQ
     LISDYFAQGK IELEKLIAGI GGADEFIKMV TDLHGKSMSG KLLLRMEN
//
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