ID   A8LLW9_DINSH            Unreviewed;       253 AA.
AC   A8LLW9;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=2-dehydro-3-deoxyglucarate aldolase {ECO:0000313|EMBL:ABV94878.1};
DE            EC=4.1.2.20 {ECO:0000313|EMBL:ABV94878.1};
GN   Name=garL {ECO:0000313|EMBL:ABV94878.1};
GN   OrderedLocusNames=Dshi_3145 {ECO:0000313|EMBL:ABV94878.1};
OS   Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV94878.1, ECO:0000313|Proteomes:UP000006833};
RN   [1] {ECO:0000313|Proteomes:UP000006833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16493 / NCIMB 14021 / DFL 12
RC   {ECO:0000313|Proteomes:UP000006833};
RX   PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA   Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA   Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA   Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA   Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA   Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA   Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA   Zech H., Simon M.;
RT   "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT   a hitchhiker's guide to life in the sea.";
RL   ISME J. 4:61-77(2010).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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DR   EMBL; CP000830; ABV94878.1; -; Genomic_DNA.
DR   RefSeq; WP_012179805.1; NC_009952.1.
DR   AlphaFoldDB; A8LLW9; -.
DR   STRING; 398580.Dshi_3145; -.
DR   KEGG; dsh:Dshi_3145; -.
DR   eggNOG; COG3836; Bacteria.
DR   HOGENOM; CLU_059964_3_2_5; -.
DR   OrthoDB; 9802624at2; -.
DR   Proteomes; UP000006833; Chromosome.
DR   GO; GO:0008672; F:2-dehydro-3-deoxyglucarate aldolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR   PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ABV94878.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006833}.
FT   DOMAIN          20..240
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   253 AA;  26522 MW;  2E6A6B50C6C7B20B CRC64;
     MRPNKLRTLL AQDTPIVNAW LSIPSGYVAE GAGHQGFDSV TVDLQHGLIG FETAVSMLQA
     ISATEAVPLV RSPSKAPEVI MHLLDAGAYG VICPMISTPE EAAAFVAACR YPPQGSRSFG
     PARGKLYGGP DYFEAANAEI LAIPMIETAE AVDRIEAILA VPGVDMIYVG PNDLALDLGE
     GPGAEWHPRA TTDAIAHVLD RARAAGVATG IFCGDGALSR QRLAEGFDLV TPGNDFNLLM
     GAMSAAIAET RRP
//