ID Q6LG39_PHOPR Unreviewed; 660 AA.
AC Q6LG39;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=5'-nucleotidase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=PBPRB1892 {ECO:0000313|EMBL:CAG23741.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG23741.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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DR EMBL; CR378680; CAG23741.1; -; Genomic_DNA.
DR RefSeq; WP_011221881.1; NC_006371.1.
DR AlphaFoldDB; Q6LG39; -.
DR STRING; 298386.PBPRB1892; -.
DR KEGG; ppr:PBPRB1892; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_7_1_6; -.
DR Proteomes; UP000000593; Chromosome 2.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 26..660
FT /note="5'-nucleotidase"
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5005144047"
FT DOMAIN 32..268
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 416..575
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 660 AA; 71869 MW; B397CC6DAD6E145D CRC64;
MTFFKPLTAL SVALILAGCS QSSQPDAVFN LTVAHINDTH SNFDPVKSSF EANGNKVYNE
FGGYPRLLTM ADEYQQDAKQ KNDSFLFLHG GDAWQGSAYF KLNQGAMNAE LLSKMGIDAM
ALGNHEFDLN NKKLNEFIGS INFPVLAVNI DASEDADLKD QTNLRPFMVY AFDGNQKVVV
DDLDKLPTDK DLVAVFGIAL DDMANISPNT GDVQFFNMVE SAQTTVDMLK AKGINNIVAV
THIGNSIDVD IASKVNGIDL IVGGHSHTLL GDFTNLGMNN DGIYAQLVKN PNGVGQTCVV
QAGQYAQAIG RLQVGFNQQG DVVNCNGKNT LLSNDEFYTQ PARQVNEKFD AAATQRVVEF
IEQEDNIEIT NEDANMRNLI NVKYKPAVDK AYGKTIAQVP VELIHERRPG DRGTDKHGSD
VAPLIAEGQY YWANTAAVQK VTGMKVDFSL IGAGGIRTNI EAGEYREGNV SLEMLPFSNF
MSVLPVKGAV IKALIDSTVT ATLPEGSHAG KFPYGGHIRY SFTETKAQEA GKIDAVEIMT
GTEASPVWTK IEDNKVYNIA LNNYNATGND GWTPLYEAQK NNSGRVDLAY VDGKLIGFDV
KNIAKVGNKY KVNYQGAAPN CKAVNTVCNT DAQAMIDYIA AERQTVTPLS YEVVTFNRAQ
//
