ID D3S920_THISK Unreviewed; 254 AA.
AC D3S920;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Short-chain dehydrogenase/reductase SDR {ECO:0000313|EMBL:ADC71525.1};
GN OrderedLocusNames=TK90_1010 {ECO:0000313|EMBL:ADC71525.1};
OS Thioalkalivibrio sp. (strain K90mix).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC71525.1, ECO:0000313|Proteomes:UP000009099};
RN [1] {ECO:0000313|Proteomes:UP000009099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K90mix {ECO:0000313|Proteomes:UP000009099};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.;
RT "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADC71525.1, ECO:0000313|Proteomes:UP000009099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K90mix {ECO:0000313|EMBL:ADC71525.1,
RC ECO:0000313|Proteomes:UP000009099};
RX PubMed=22675584; DOI=10.4056/sigs.2315092;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Foster B., Sun H.,
RA Ivanova N., Pati A., D'haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of Thioalkalivibrio sp. K90mix.";
RL Stand. Genomic Sci. 5:341-355(2011).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR EMBL; CP001905; ADC71525.1; -; Genomic_DNA.
DR RefSeq; WP_012982419.1; NC_013889.1.
DR AlphaFoldDB; D3S920; -.
DR STRING; 396595.TK90_1010; -.
DR KEGG; tkm:TK90_1010; -.
DR eggNOG; COG0300; Bacteria.
DR HOGENOM; CLU_010194_2_1_6; -.
DR OrthoDB; 335726at2; -.
DR Proteomes; UP000009099; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR44196; DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 7B; 1.
DR PANTHER; PTHR44196:SF1; DEHYDROGENASE_REDUCTASE SDR FAMILY MEMBER 7B; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 254 AA; 27592 MW; 2EFB11B8C74E1DED CRC64;
MNRLQSVVIL GATSAIATAV ARELAEHGAR LFLVARDGER LEPLLQDLRV RGDDASGTRI
LGTTADLADI DAHADVWAQA REALSDNIDA VLLAWGTLPD QEACNTSVAT TLEAIHVNGT
SAIAFLACIA PDFEQRGRGV IAAIGSVAGD RGRQSNYVYG TAKGMLATYL QGLRNRLFFS
GVDVVTIKPG FVRTPMTEGF NRAGALWAEP DTVARGIVKA MRRGRDVAYL PWIWWGIMTV
IRLIPEYLFK RLKL
//
