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Database: UniProt
Entry: A0A1M5KW73_9BACT
LinkDB: A0A1M5KW73_9BACT
Original site: A0A1M5KW73_9BACT 
ID   A0A1M5KW73_9BACT        Unreviewed;       732 AA.
AC   A0A1M5KW73;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Rhamnulose-1-phosphate aldolase/alcohol dehydrogenase {ECO:0000313|EMBL:SHG56997.1};
GN   ORFNames=SAMN05443144_1358 {ECO:0000313|EMBL:SHG56997.1};
OS   Fodinibius roseus.
OC   Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX   NCBI_TaxID=1194090 {ECO:0000313|EMBL:SHG56997.1, ECO:0000313|Proteomes:UP000184041};
RN   [1] {ECO:0000313|EMBL:SHG56997.1, ECO:0000313|Proteomes:UP000184041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21986 {ECO:0000313|EMBL:SHG56997.1,
RC   ECO:0000313|Proteomes:UP000184041};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; FQUS01000035; SHG56997.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5KW73; -.
DR   STRING; 1194090.SAMN05443144_1358; -.
DR   OrthoDB; 9774430at2; -.
DR   Proteomes; UP000184041; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; PTHR43008; BENZIL REDUCTASE; 1.
DR   PANTHER; PTHR43008:SF4; CHAIN DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G08710)-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   SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          30..239
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   732 AA;  80620 MW;  AD86F372F4B34FAD CRC64;
     METSTTQKYF RRVESKWDDR EAKGKDPLAS LVYRSNLLGS DSYINNTGGG NTSSKVMEED
     PISGQEAEVL WVKGSGGDLR TATKPNFASL YQQKLLKLQD IYHSMENTGL KTPAEDSMTE
     MYPHCTFNLN PRAPSIDTPL HSFIPYKYVD HTHPVPVIAI ATADNGPELM REVYGDEVEW
     VDWMRPGFEL GLKLQEVIEE NPGIRGIILG GHGLINWADD EKECYETSIE LINKAADYLN
     EHERGEDSFG GSRYKSLEKE ERREVLADIL PFLRGQVSQE NQFIGTVQDD EVTLQFINAE
     DAPRLAELGT SCPDHFLRTK IKPLYVEWNP QEDSMEDLKG AITAGLQQYR EDYAKYYNSH
     RDEDSPDMRD PNPTVILIPG LGMIAWGKNK SESRVTAEFY TAAIGVMRGA ESVANYTALP
     KQEAYDIEYW ALEEAKLQRM PPESELSRQV IAVIGAGSGI GKALVSRLIK EGGTVAALDL
     HEDTAKATAE DVLEEIGMGI GVAGSDISGS GDVIGLGCDI TDRQSVQQAL HDITIAYGGL
     DNVAVTAGLY PTPDQNGDVK DAGWDNSFAV NVKGNYIVAD EVADIWEAQN LDGSMVITTS
     ANAVVPKAGS MAYDTSKSAA NHLIRELAIA LAPRVRVNGV APATVVEGSS MFPRDRVIAS
     LKKYGLDFDE EESTETLRET LADFYASRTL TRQPITLDQQ TEAIYSLISS RYENTTGHII
     PVDGGLKEAF LR
//
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