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Database: UniProt
Entry: A0A239E2F3_9SPHN
LinkDB: A0A239E2F3_9SPHN
Original site: A0A239E2F3_9SPHN 
ID   A0A239E2F3_9SPHN        Unreviewed;       443 AA.
AC   A0A239E2F3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Pro-Hyp dipeptidase. Metallo peptidase. MEROPS family M38 {ECO:0000313|EMBL:SNS38458.1};
GN   ORFNames=SAMN06295955_101549 {ECO:0000313|EMBL:SNS38458.1};
OS   Sphingopyxis indica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=436663 {ECO:0000313|EMBL:SNS38458.1, ECO:0000313|Proteomes:UP000198339};
RN   [1] {ECO:0000313|EMBL:SNS38458.1, ECO:0000313|Proteomes:UP000198339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS15 {ECO:0000313|EMBL:SNS38458.1,
RC   ECO:0000313|Proteomes:UP000198339};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZPA01000001; SNS38458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239E2F3; -.
DR   OrthoDB; 9782972at2; -.
DR   Proteomes; UP000198339; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01299; Met_dep_hydrolase_A; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198339};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..443
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013031735"
FT   DOMAIN          90..440
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   443 AA;  47463 MW;  E0BFE31D52CA1B4C CRC64;
     MRYRVKSGSF LRRVGFAAAA LGATGAMAQE DVAGQQTVIT AAHMLDVQSG KTIDYPAIFV
     GADGRITNIA DARTVRWGEG VKHIDLGDRT LLPGLIDMHV HLDGPADIGG YRGLEFTDSF
     WGMTAVKNAR DMLDAGFTTV RNVGSDNRND IGLKQAIDAG YAVGPRIVPA GYALGATGGH
     CDSTFLPPSL EKADGKEEGI GDTPDELRYQ VRRQRKYGAE VIKVCATGGV FSRNTEPGQL
     QVPENELRAI ADEAHQWGLR VAAHAHGAAG IRTAIAAGID TIEHASLVDD EGIRMAVTRK
     RPVWFGMDIY NTEYTQAEGA KNGVLEDNLR KDREIAQIQR DNFRKAHRAG VRMVFASDAG
     VMPHGDVGKQ FRVMVEYGMT PMQAIQAATK NAAEALGREG DVGAIAVGRY ADIVAVDGDP
     LANIRELESV DAVLKGGVLV KGE
//
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