ID V6M596_9BACL Unreviewed; 689 AA.
AC V6M596;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:EST53776.1};
GN ORFNames=T458_23745 {ECO:0000313|EMBL:EST53776.1};
OS Brevibacillus panacihumi W25.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1408254 {ECO:0000313|EMBL:EST53776.1, ECO:0000313|Proteomes:UP000017973};
RN [1] {ECO:0000313|EMBL:EST53776.1, ECO:0000313|Proteomes:UP000017973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W25 {ECO:0000313|EMBL:EST53776.1,
RC ECO:0000313|Proteomes:UP000017973};
RX PubMed=24459276;
RA Wang X., Jin D., Zhou L., Wu L., An W., Chen Y., Zhao L.;
RT "Draft Genome Sequence of Brevibacillus panacihumi Strain W25, a
RT Halotolerant Hydrocarbon-Degrading Bacterium.";
RL Genome Announc. 2:e01215-13(2014).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:EST53776.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYJU01000017; EST53776.1; -; Genomic_DNA.
DR RefSeq; WP_023558542.1; NZ_KI629785.1.
DR AlphaFoldDB; V6M596; -.
DR STRING; 1408254.T458_23745; -.
DR PATRIC; fig|1408254.3.peg.4667; -.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3347; Bacteria.
DR HOGENOM; CLU_024866_0_0_9; -.
DR OrthoDB; 9774430at2; -.
DR Proteomes; UP000017973; Unassembled WGS sequence.
DR CDD; cd08943; R1PA_ADH_SDR_c; 1.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR013454; Bifunc_RhaD/ADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR NCBIfam; TIGR02632; RhaD_aldol-ADH; 1.
DR PANTHER; PTHR43669; 5-KETO-D-GLUCONATE 5-REDUCTASE; 1.
DR PANTHER; PTHR43669:SF8; SHORT-CHAIN TYPE DEHYDROGENASE_REDUCTASE-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM01007; Aldolase_II; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017973}.
FT DOMAIN 20..219
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 689 AA; 75801 MW; 673235836E09FB4F CRC64;
MIRSLWDRDQ ADHLQSGLEE LVYRSNLIGA DRRVCNWGGG NTSTKTKGTD FRGREIDIMW
VKGSGSDLAT MKAHQFTGLR LDDVLPLLAR EEMSDEEMVA YLAHCMIDSK HPRPSIETLL
HAFLPFPHVD HTHPDAIISI CCADNGREVA REIFGDRFVW VPYVRPGFTL SKMIAEGVAQ
NPQAELVLME KHGLVTWGET AEQCYAKTIA VIQEAERFIA ARVQKDQVFG GQVCESLPEP
ERKEVLAQLM PLIRGAVSGQ KRMILTFDDA QDVLAFVNSK EGKTLSQIGA ACPDHLVHTK
MVPLFVEWDP ATRDVGVLKQ QLRDGIDRYQ REYQAYFERN HSEGDQMSET APRVILIPGI
GMINTGKSWA ASKVSGALYH RAIAVMRGAT ALGDFVSLSE QESYLVEYWP LELYKLTLAP
PEAEFSRQVV FVTGGAGGIG SETCRSFVAQ GAHVVVADLN IDGARQVADE INARYGDGRA
IAVKMDVTRE EEVVAALKEA ALAYGGIDVV VNNAGLATSS PFDETTLQEW ELNISVLGTG
YFLVAREAFK QMKAQGIGGN MVFVGSKNSV YAGKNVSAYS SAKALEVHLA RCIAAEGGEY
GIRVNSILPD AILQGSAIWN SSWRNERAAA YGIKPDELEE YYRKRTTLLV NIYPKDIAEG
ILFFASSRSE KTTGCMLTID GGVQAAFTR
//