ID A0A0S9BZ88_9MICC Unreviewed; 678 AA.
AC A0A0S9BZ88;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:KQN86743.1};
GN ORFNames=ASE96_14070 {ECO:0000313|EMBL:KQN86743.1};
OS Arthrobacter sp. Leaf69.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN86743.1, ECO:0000313|Proteomes:UP000051467};
RN [1] {ECO:0000313|EMBL:KQN86743.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN86743.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN86743.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN86743.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Schulze-Lefert P.;
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:KQN86743.1}.
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DR EMBL; LMLR01000013; KQN86743.1; -; Genomic_DNA.
DR RefSeq; WP_056432240.1; NZ_LMLR01000013.1.
DR AlphaFoldDB; A0A0S9BZ88; -.
DR STRING; 1736232.ASE96_14070; -.
DR OrthoDB; 9774430at2; -.
DR Proteomes; UP000051467; 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 8..210
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT REGION 17..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 71460 MW; 73F20AF2A5F85C62 CRC64;
MTNPTVEQLV ARSNRLGADK RNTNFAGGNT SAKGTDKDPV TGEDVQLLWV KGSGGDLGTL
TGSGLAVLRL DRLNALKNVY PGVEREDEMV AAFDYCLHGK GGAAPSIDTA MHGLVDAAHV
DHLHPDAGIA IATAADGEAL TKEIFGEKVA WVPWRRPGFQ LGLDIAAIKD ANPRAVGTIL
GGHGTTAWGD TSEEAETNSL WIIEQAEKYI AEHGRPEPFG AKLPGYAALP EAERRAKAAA
LAPVIRGLAS SDKPVVGHFT DDAAILDFLE GAEHPRLGAL GTSCPDHFLR TKVKPLVLDL
PADASVEESI ARLKELHAAY RVDYQAYYDR HADADSPALR GADPAIVLVP GVGMFSYGKD
KQTARVAGEY YRNAINVMRG AEAVSRYAPI EESEKFRIEY WALEEAKLAR MPKPKSHAGR
IALVTGAASG IGKAIATRLA AEGACVVIAD LNLDSARAVA AELGGSDVAV GIKADVTDEA
QVVAAVNAAV LAFGGLDLVV NNAGLSISKP LLETTEKDWD IQHNVMAKGS FLVSKAAAKV
LIDQGMGGDI VYISSKNSVF AGPNNIAYSA TKADQAHQVR LLAAELGEFG IRVNGINPDG
VVRGSGIFAG GWGAKRAAVY GVDEQDLGKY YAQRTLLKRE VLPENVANAV SVLTSDELSH
TTGLHIPVDA GVATAFLR
//
