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Database: UniProt
Entry: D2R6A3_PIRSD
LinkDB: D2R6A3_PIRSD
Original site: D2R6A3_PIRSD 
ID   D2R6A3_PIRSD            Unreviewed;       265 AA.
AC   D2R6A3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=HpcH/HpaI aldolase {ECO:0000313|EMBL:ADB15481.1};
GN   OrderedLocusNames=Psta_0796 {ECO:0000313|EMBL:ADB15481.1};
OS   Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS   staleyi).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Pirellula.
OX   NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB15481.1, ECO:0000313|Proteomes:UP000001887};
RN   [1] {ECO:0000313|EMBL:ADB15481.1, ECO:0000313|Proteomes:UP000001887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC   {ECO:0000313|Proteomes:UP000001887};
RX   PubMed=21304671; DOI=10.4056/sigs.51657;
RA   Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA   Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL   Stand. Genomic Sci. 1:308-316(2009).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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DR   EMBL; CP001848; ADB15481.1; -; Genomic_DNA.
DR   RefSeq; WP_012909746.1; NC_013720.1.
DR   AlphaFoldDB; D2R6A3; -.
DR   STRING; 530564.Psta_0796; -.
DR   KEGG; psl:Psta_0796; -.
DR   eggNOG; COG3836; Bacteria.
DR   HOGENOM; CLU_059964_4_0_0; -.
DR   OrthoDB; 86160at2; -.
DR   Proteomes; UP000001887; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT   DOMAIN          49..245
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   265 AA;  28763 MW;  306C1C99056F4322 CRC64;
     MASAPPSFRS IKQRLQAGEP VNVFCVGRLI HPVIFDLHGM LGGFHGCWID QEHAATTYEQ
     IVLASACCRA QGMDSFVRMP MTGYAQATAN LEAGTGGLMA ARIDTAAEAE TFVSWAKFAP
     RGRRGLNTSG FDADYGALSL AELAQRANER NLVAIQIETE GALAECEAIA AIQDVDMLFV
     GPSDLSQELG VIGNWESEKL WSAYERVAAA CQQHKKSWGT IAVNPTFARR VQSLGCQLLS
     FGMDAIIYRR GIEGTKRSFE GFFEA
//
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