ID A0A0R2MUC2_9LACO Unreviewed; 251 AA.
AC A0A0R2MUC2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Carbonyl reductase {ECO:0000313|EMBL:KRO15155.1};
GN ORFNames=IV56_GL000246 {ECO:0000313|EMBL:KRO15155.1};
OS Lacticaseibacillus saniviri JCM 17471 = DSM 24301.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1293598 {ECO:0000313|EMBL:KRO15155.1, ECO:0000313|Proteomes:UP000050969};
RN [1] {ECO:0000313|EMBL:KRO15155.1, ECO:0000313|Proteomes:UP000050969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24301 {ECO:0000313|EMBL:KRO15155.1,
RC ECO:0000313|Proteomes:UP000050969};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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:KRO15155.1}.
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DR EMBL; JQCE01000075; KRO15155.1; -; Genomic_DNA.
DR RefSeq; WP_054776729.1; NZ_JQCE01000075.1.
DR AlphaFoldDB; A0A0R2MUC2; -.
DR STRING; 1293598.IV56_GL000246; -.
DR PATRIC; fig|1293598.4.peg.265; -.
DR OrthoDB; 5786478at2; -.
DR Proteomes; UP000050969; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05324; carb_red_PTCR-like_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045313; CBR1-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43963:SF4; CARBONYL REDUCTASE (NADPH); 1.
DR PANTHER; PTHR43963; CARBONYL REDUCTASE 1-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050969}.
SQ SEQUENCE 251 AA; 26922 MW; 58C07DB7E85DA4AF CRC64;
MTNTTISLVT GANRGMGLEI VKELATAGQT VLLGSRDLNK GQEAAQKLAA EGLAVEAIQL
DITDTDAITR AVDFVSNKYG RLDVLINNAG ASFDKFQDPS ILKLDVIRRE FELNVFGTID
MTQQFIPLLK KSPNAKIINI SSMMGSLTEA LNPQSSVYNA SSMGYQATKS ALNMFTVQLA
KEFQRKDIPI TVNAIDPGLV ATEFGGTSAD SALEYGAQPV EVGVARTVEL VTSPDNDITA
TFSNTHGEVN W
//
