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Database: UniProt
Entry: R7ZMF0_9BACT
LinkDB: R7ZMF0_9BACT
Original site: R7ZMF0_9BACT 
ID   R7ZMF0_9BACT            Unreviewed;       702 AA.
AC   R7ZMF0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Putative rhamnulose-1-phosphate aldolase {ECO:0000313|EMBL:EON75278.1};
DE            EC=1.2.1.22 {ECO:0000313|EMBL:EON75278.1};
DE            EC=4.1.2.19 {ECO:0000313|EMBL:EON75278.1};
GN   ORFNames=ADIS_4449 {ECO:0000313|EMBL:EON75278.1};
OS   Lunatimonas lonarensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX   NCBI_TaxID=1232681 {ECO:0000313|EMBL:EON75278.1, ECO:0000313|Proteomes:UP000013909};
RN   [1] {ECO:0000313|EMBL:EON75278.1, ECO:0000313|Proteomes:UP000013909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK24 {ECO:0000313|EMBL:EON75278.1,
RC   ECO:0000313|Proteomes:UP000013909};
RA   Singh A.;
RT   "A novel strain isolated from Lonar lake, Maharashtra, India.";
RL   Submitted (FEB-2013) 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:EON75278.1}.
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DR   EMBL; AQHR01000110; EON75278.1; -; Genomic_DNA.
DR   RefSeq; WP_010856562.1; NZ_AQHR01000110.1.
DR   AlphaFoldDB; R7ZMF0; -.
DR   STRING; 1232681.ADIS_4449; -.
DR   PATRIC; fig|1288963.3.peg.4438; -.
DR   OrthoDB; 9774430at2; -.
DR   Proteomes; UP000013909; Unassembled WGS sequence.
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   SMART; SM00822; PKS_KR; 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:EON75278.1};
KW   Oxidoreductase {ECO:0000313|EMBL:EON75278.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013909}.
FT   DOMAIN          30..232
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   702 AA;  76927 MW;  5E3942E4B0ADBC68 CRC64;
     MSVSEKSFKH VNYLWDKEKE KELGDDQVAL LLYRSNILGS DLRITNYGGG NTSCKTMEID
     PLTKEKTEVM WIKGSGGDIG TLKRSGLAGL YQEKLHSLKN VYRGLEFEDE MVGLFNHCIY
     DLDSKAPSID TPLHAFLPFK HIDHLHPDAA IAIAASKDGE KITQELFEGQ IAWVPWQRPG
     FDIALKLEKA VQDNPGIRGI MLGGHGLFTW GDTAYECYIN SLEVIEKASQ YLEDNYGKSR
     PVFGGQRVQS LEADQRQDQA AKIAPILRGL ASSYNRMVGT FTDDARVLEF INSHDLDKLA
     PLGTSCPDHF LRTKIRPLVL DIPADYDLSD GAALKEKLEV EFQKYREYYV NYYEDHKHPN
     SPGVRDSNPV IILWPGIGMF SYAKDKQTSR VASEFYINAI NVMKGAEAIS EYVALPLQEA
     FDIEYWLLEE AKLQRMPKEK PLSRKIAFVT GGAGGIGKAI ADRLAAEGAC VFITDINKDN
     LDAAVATYNR DTGAGTLMDV TSMADIERAL KETILKFGGV DVVVNCAGLA ISKPIDQTSE
     KEWDLLQDVL VKGQFAVSKA AVAILRAQNK GGDIINIASK NALVSGPNNV GYGTAKAAQV
     HMSRLLAAEL GPDKIRVNVV NPDAVIEGSK IWEGAWAAGR AKAYGISIEE LPAFYAKRTI
     MNEIISTADI ASAVFAFVGG DLSKSTGNIL NVDGGVAAAF VR
//
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