ID Q6AAK1_CUTAK Unreviewed; 404 AA.
AC Q6AAK1;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Dehydrogenase, putative myo-inositol 2-dehydrogenase {ECO:0000313|EMBL:AAT82215.1};
DE EC=1.1.1.18 {ECO:0000313|EMBL:AAT82215.1};
GN OrderedLocusNames=PPA0463 {ECO:0000313|EMBL:AAT82215.1};
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT82215.1, ECO:0000313|Proteomes:UP000000603};
RN [1] {ECO:0000313|EMBL:AAT82215.1, ECO:0000313|Proteomes:UP000000603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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DR EMBL; AE017283; AAT82215.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6AAK1; -.
DR EnsemblBacteria; AAT82215; AAT82215; PPA0463.
DR KEGG; pac:PPA0463; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_023194_17_0_11; -.
DR Proteomes; UP000000603; Chromosome.
DR GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR PANTHER; PTHR43818:SF11; BCDNA.GH03377; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:AAT82215.1}.
FT DOMAIN 16..143
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 156..398
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 404 AA; 42936 MW; DED4495C1AFE3290 CRC64;
MSALSQPATS QRHPLSVAVI GAGMAGRTHA NAWRQVGTVF GSEGIPPIRL AAICDSYEPF
ARSARDSYGY ERAVTDWHDI VDADDIDVVS VVVSNALHRQ VAEDLVRAGK HVLCEKPLSD
SLKNARAMAE LEANSQVVTG VGFSYRRHPS VAAIAELVRQ GRLGDVTTFS GRYWCGYGVD
PTVPMAWRYR GPQGSGALGD LGSHIIDVAE FVCGPIRSVR GGAFATIIDK RPPALEGVAG
GRGMTVSAQA IETVENDDIA VFNMTFESGA IGTIVVSRVA FGLPNSMEFD VFGTQGRASF
DLARSGEIIV DDTSTPEGFS GPRQVLSNPT FPYYKGGSSM DFAGVGSTQI EQFTYQARAF
LDQVLGLDEG FPLVPSFAHG YRTMCIADAV ARSAAAGGKT IDLT
//
