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Database: UniProt
Entry: A0A0S9DBN0_9MICC
LinkDB: A0A0S9DBN0_9MICC
Original site: A0A0S9DBN0_9MICC 
ID   A0A0S9DBN0_9MICC        Unreviewed;       695 AA.
AC   A0A0S9DBN0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:KQO03322.1};
GN   ORFNames=ASF21_03180 {ECO:0000313|EMBL:KQO03322.1};
OS   Arthrobacter sp. Leaf234.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQO03322.1, ECO:0000313|Proteomes:UP000053418};
RN   [1] {ECO:0000313|Proteomes:UP000053418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQO03322.1}.
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DR   EMBL; LMLU01000001; KQO03322.1; -; Genomic_DNA.
DR   RefSeq; WP_055766678.1; NZ_LMLU01000001.1.
DR   AlphaFoldDB; A0A0S9DBN0; -.
DR   STRING; 1736303.ASF21_03180; -.
DR   Proteomes; UP000053418; Unassembled WGS sequence.
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; PF13561; adh_short_C2; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
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;
FT   DOMAIN          25..227
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          28..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   695 AA;  73348 MW;  87FAA73C2D444D48 CRC64;
     MTVTTTTGPA TDATTNPTVN RTVQELIERS NRLGSDKRTT NYAGGNTSAK GVGTDPVTGE
     DVELLWVKGS GGDLGTLKAA GLAVLRLDRM RALQGVYPGV EREDEMVAAF DYTLHGKGGA
     APSIDTAMHG LVDAAHVDHL HPDAGIAIAT SADGEALTTA IFGPKVLWVP WRRPGFQLGL
     DIAAIKDAHP EAIGTILGGH GITAWGDTSA EAEANSLWII ETAERYIAEH GTPEPFGPAL
     EGYGPLPEDE RRARAAALAP TIRGLASTDR AQVGHFTDDP RVLEFLASSG HPRLGALGTS
     CPDHFLRTKV KPLVLDLPAD ADVESCLLRL RELHTEYRTD YAAYYDRHAT PDSPPMRGAD
     PAIVLVPGVG MFSFGANKQT ARVAGEFYLN AINVMRGAEA VSTYAPIEES EKFRIEYWSL
     EEAKLARMPK PKSHAGRIAL VTGAASGIGR AIATRLAAEG ACVVIADLNI DSASSVAQDL
     GGPDVAIGVQ ADVTDPAQVL RAVQAAVLAF GGLDLVVNNA GLSISKPLLE TTEKDWDLQH
     DVMAKGSFLM SQAAAKVLIE QDMGGDIIYI SSKNSVFAGP NNIAYSATKA DQAHQVRLLA
     AELGEYGVRV NGINPDGVVR GSGIFAGGWG AKRAAVYGVD EEKLGEYYAQ RTLLKREVLP
     ENVANAVAVL TSDELSHTTG LHIPVDAGVA AAFLR
//
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