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Database: UniProt
Entry: A3XPK7_LEEBM
LinkDB: A3XPK7_LEEBM
Original site: A3XPK7_LEEBM 
ID   A3XPK7_LEEBM            Unreviewed;       698 AA.
AC   A3XPK7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Class II aldolase/adducin N-terminal domain-containing protein {ECO:0000259|SMART:SM01007};
GN   ORFNames=MED217_13434 {ECO:0000313|EMBL:EAQ48512.1};
OS   Leeuwenhoekiella blandensis (strain CECT 7118 / CCUG 51940 / KCTC 22103 /
OS   MED217) (Flavobacterium sp. (strain MED217)).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Leeuwenhoekiella.
OX   NCBI_TaxID=398720 {ECO:0000313|EMBL:EAQ48512.1, ECO:0000313|Proteomes:UP000001601};
RN   [1] {ECO:0000313|EMBL:EAQ48512.1, ECO:0000313|Proteomes:UP000001601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED217 {ECO:0000313|EMBL:EAQ48512.1,
RC   ECO:0000313|Proteomes:UP000001601};
RX   PubMed=17215843; DOI=10.1038/nature05381;
RA   Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA   Neutze R., Pedros-Alio C., Pinhassi J.;
RT   "Light stimulates growth of proteorhodopsin-containing marine
RT   Flavobacteria.";
RL   Nature 445:210-213(2007).
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:EAQ48512.1}.
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DR   EMBL; AANC01000008; EAQ48512.1; -; Genomic_DNA.
DR   RefSeq; WP_009781041.1; NZ_CH672395.1.
DR   AlphaFoldDB; A3XPK7; -.
DR   STRING; 398720.MED217_13434; -.
DR   eggNOG; COG1028; Bacteria.
DR   eggNOG; COG3347; Bacteria.
DR   HOGENOM; CLU_024866_0_0_10; -.
DR   OrthoDB; 9774430at2; -.
DR   Proteomes; UP000001601; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000001601}.
FT   DOMAIN          27..229
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   698 AA;  76387 MW;  618373A39FCB1A31 CRC64;
     MEKTFSHVDY LWDEQKAAEL GDDQVALFLY RSNILGADLR ITNYGGGNTS CKTIEKDPLT
     NEDVEVMWVK GSGGDIGTLT RQGIAGLYTE RLRNLKNVYG GLEDEDRMVG LFNHCIYDLD
     SKAPSIDTPL HGLLPFAHID HLHPDALIAI AAAEDSEKIT KEIWGDTMGW VPWQRPGFDL
     GLQLEKCLNE NPGIRGIVLG SHGLFTWGDT SYECYINSLE VIEKASSYIE KKVKENGSVF
     GGQKIESLPA DQRKDQAAKL MPLLRGLASS ENRMIGHFTD SDTVLQFINS NDLDKLAPMG
     TSCPDHFLRT KIQPLILDLD KDADLDDTEA VLAKLEPSFE QYRQEYKDYY ESCKHDNSPA
     MRDPNPVIII FPGVGMFSFA KNKQTTRVAS EFYINAINVM RGAEAITSYT SLPRQEAFDI
     EYWLLEEAKL QRMPKEQPLS RKVALVTGAA GGIGKAIADK LVAEGANVVL TDMSDEALKE
     AVATYKKDQV AGAVCDVTSE EAIKKAYKEA CLAFGGVDIV IHSAGLAISK ALEDTTQKDW
     DLLQNVLVKG QFLMAQEGVA IMRKQGLGGD IVNIASKNGL VSGPNNVGYG TAKAAQQHMT
     RLLAAELGSD KIRVNTVNPD GVIVGSKIWE GAWAEGRAKA YGIEVKDLPA HYAKRNLLNE
     IILPDDIADG VFACVGVLQK STGNTINVDG GMANAFVR
//
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