ID A0A1B1NEE3_9MICO Unreviewed; 680 AA.
AC A0A1B1NEE3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative rhamnulose-1-phosphate aldolase {ECO:0000313|EMBL:ANS79725.1};
DE EC=1.2.1.22 {ECO:0000313|EMBL:ANS79725.1};
DE EC=4.1.2.19 {ECO:0000313|EMBL:ANS79725.1};
GN ORFNames=SGUI_2329 {ECO:0000313|EMBL:ANS79725.1};
OS Serinicoccus hydrothermalis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=1758689 {ECO:0000313|EMBL:ANS79725.1, ECO:0000313|Proteomes:UP000092482};
RN [1] {ECO:0000313|EMBL:ANS79725.1, ECO:0000313|Proteomes:UP000092482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT9 {ECO:0000313|EMBL:ANS79725.1,
RC ECO:0000313|Proteomes:UP000092482};
RA Tang K.;
RT "Shallow-sea hydrothermal system.";
RL Submitted (MAR-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; CP014989; ANS79725.1; -; Genomic_DNA.
DR RefSeq; WP_066640495.1; NZ_CP014989.1.
DR AlphaFoldDB; A0A1B1NEE3; -.
DR STRING; 1758689.SGUI_2329; -.
DR KEGG; serj:SGUI_2329; -.
DR PATRIC; fig|1758689.4.peg.2428; -.
DR OrthoDB; 9774430at2; -.
DR Proteomes; UP000092482; Chromosome.
DR GO; GO:0008911; F:lactaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008994; F:rhamnulose-1-phosphate aldolase activity; IEA:UniProtKB-EC.
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 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;
KW Lyase {ECO:0000313|EMBL:ANS79725.1};
KW Oxidoreductase {ECO:0000313|EMBL:ANS79725.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092482}.
FT DOMAIN 10..212
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 71720 MW; 2B87D694ADD97133 CRC64;
MTDENPAVSD LITRSNRLGA DPKNTNYAGG NTSAKGTGTD PVTGRPVELL WVKGSGGDLG
TLKPGGLAAL RLDRMRALVD VYPGVEREDE MVAAFDYCLH GKGGAAPSID TAMHGLVEAA
HVDHLHPDSG IAIATAADGD ELTRTIFGDK VAWVPWRRPG FQLGLDIAAI KEEHPEAIGC
VLGGHGITAW GETSEECEAN SLWIIDTAAA YIEEHSTDEP FGAALEGYAA LPEPERHARA
AALAGTIRGI ASTDRPMVGH YTDSDVVLDF LAHEAHPRLA ELGTSCPDHF LRTKVKPLVL
DLPATAGVEE MKERLLELHQ PYREDYQGYY ERNATDDSPA IRGADPLIVL VPGVGMFSFG
KDKQTARVAG EFYVNAINVM RGAEGLSTYA PIDEAEKFRI EYWALEEAKL QRMPKPKPLA
TRVALVTGGA SGIGNATAQR LAAEGACVVV ADLDLEKAQA AAAEIGGPDV AVGVQVDVSD
AAAVQAAVDA AVLAFGGLDL VVNNAGLSLS KSLLDTTEAD WDRQHDVMAK GSFLVSQAAA
RVLIDQRMGG DIVYISSKNS IFAGPNNIAY SATKADQAHQ VRLLAAELGA HGVRVNGINP
DGVVAGSGIF AGGWGANRAE VYGVEEKDLG AFYAQRTILK QEVLPEHCAA AVFALVGPDL
RQTTGLHVPV DSGVAAAFLR
//
