ID E3HRX8_ACHXA Unreviewed; 640 AA.
AC E3HRX8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=5'-nucleotidase {ECO:0000313|EMBL:ADP13639.1};
DE EC=3.1.3.5 {ECO:0000313|EMBL:ADP13639.1};
GN Name=ushA {ECO:0000313|EMBL:ADP13639.1};
GN OrderedLocusNames=AXYL_00279 {ECO:0000313|EMBL:ADP13639.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP13639.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP13639.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP13639.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|ARBA:ARBA00006654, ECO:0000256|RuleBase:RU362119}.
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DR EMBL; CP002287; ADP13639.1; -; Genomic_DNA.
DR RefSeq; WP_013391038.1; NC_014640.1.
DR AlphaFoldDB; E3HRX8; -.
DR STRING; 762376.AXYL_00279; -.
DR KEGG; axy:AXYL_00279; -.
DR PATRIC; fig|762376.5.peg.280; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_7_1_4; -.
DR OrthoDB; 9803927at2; -.
DR Proteomes; UP000006876; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
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; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575:SF24; 5'-NUCLEOTIDASE; 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; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362119};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362119}; Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 21..640
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5005127784"
FT DOMAIN 48..280
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 440..589
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 640 AA; 66465 MW; 06159A30309A3CB6 CRC64;
MNTWKRNAGA AMLSALALLA GCGGGDDDDD KPVEQPEQPV PGRAMELTIL HINDHHSNLD
SKKKDLKLKT ASGSRVAVNA DTGGFPRVTG AINALASQSA NVLKLHAGDA TTGTLYFNRA
GEPGEADAAM MNTVCFDAMT LGNHEFDKGD SGLKRFIDLL HAGACQTPVL SANVTFAAGS
ALNPSRAPGM VKPAVVLKRD GQDIGLVGLT IAAKTQQSSS PDAGTVFSDE TAAAQQQIDA
LRAQGVNKIV VMSHIGYDYD KQVIAQLSGV DVVVGGDSHT LLGPASMADY GVGSPAGAYP
TVLQDKDGKR VCLVQAWEYS QVVGELKVSF DANGDVTACA GTPHVLMDGP LKVAGAAPSA
ADEAAIQADV LASGFLRMQA PDAQATAVLQ PFKAKVDQFS RSLVASVPQE LCSRRVPGGP
GSRDYSRSSA ACNTLGSVSL RGGDIQQLVA QAYLDVANAS YGGADISLQS GGGVRVPLLG
NVTAANVIEV VPFGNMLWRL DVTGAEVKSM LEDGMQAVYG AGGSTGPYPY AGGLRWDVNA
AQAQGNRVSN IEVRDQASGN WLPLDASRSY KLFVLSFNAT GGDGYKTLAN VPASRRQDIG
VLDADVLQAY IDKQAKDPAS GLPVLNLLPA SLYSTKTYSE
//