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
//