ID   YPRB2_CORML             Reviewed;         304 AA.
AC   P0C1E9; P45637;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Uncharacterized protein in proB 3'region;
DE            EC=1.-.-.-;
OS   Corynebacterium melassecola.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=41643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17965 / AS B-4821;
RX   PubMed=8755867; DOI=10.1128/jb.178.15.4412-4419.1996;
RA   Ankri S., Serebrijski I., Reyes O., Leblon G.;
RT   "Mutations in the Corynebacterium glutamicum proline biosynthetic pathway:
RT   a natural bypass of the proA step.";
RL   J. Bacteriol. 178:4412-4419(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 229-304.
RC   STRAIN=ATCC 17965 / AS B-4821;
RX   PubMed=8522535; DOI=10.1128/jb.177.24.7255-7260.1995;
RA   Serebrijski I., Wojcik F., Reyes O., Leblon G.;
RT   "Multicopy suppression by asd gene and osmotic stress-dependent
RT   complementation by heterologous proA in proA mutants.";
RL   J. Bacteriol. 177:7255-7260(1995).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; U31230; AAC44175.1; -; Genomic_DNA.
DR   EMBL; X82929; CAA58102.1; -; Genomic_DNA.
DR   PIR; S49979; S49979.
DR   PIR; T50667; T50667.
DR   AlphaFoldDB; P0C1E9; -.
DR   SMR; P0C1E9; -.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..304
FT                   /note="Uncharacterized protein in proB 3'region"
FT                   /id="PRO_0000236033"
FT   ACT_SITE        217
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..137
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..217
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         265..268
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   304 AA;  33037 MW;  601C37DD5BCAD6E7 CRC64;
     MKFVMYPHLW ESTTAVIEGG GHERVEDIKD ADFIFFNGSA PEFPDLPENI KFVQASMAGI
     DALVKRGVVN EKARWANAAG LYADTVAEST IGLILAQMHM HAATRLAKSW SVRPEVENNK
     SWLHDNKTVA ILGAGGIGVR LLEMLKPFNV KTIAVNNSGR PVEGADETFA MDKAEHVWAE
     ADVFVLILPL TDATYQIVNA ETLGKMKPSA VLVNVGRGPL INTDDLVDAL NNGTIAGAAL
     DVTDPEPLPD SHPLWEMDNV VITPHTANTN ERIRALTGEL TLRNIELFEA GEQMATEVDV
     VAGY