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}.
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; 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
//