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Database: UniProt
Entry: A0A0A7RZK9_FRIPE
LinkDB: A0A0A7RZK9_FRIPE
Original site: A0A0A7RZK9_FRIPE 
ID   A0A0A7RZK9_FRIPE        Unreviewed;       573 AA.
AC   A0A0A7RZK9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Putative metal-dependent hydrolase with the TIM-barrel fold {ECO:0000313|EMBL:AJA44729.1};
GN   ORFNames=FPB0191_00903 {ECO:0000313|EMBL:AJA44729.1};
OS   Frischella perrara.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Orbales; Orbaceae;
OC   Frischella.
OX   NCBI_TaxID=1267021 {ECO:0000313|EMBL:AJA44729.1, ECO:0000313|Proteomes:UP000030901};
RN   [1] {ECO:0000313|EMBL:AJA44729.1, ECO:0000313|Proteomes:UP000030901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEB0191 {ECO:0000313|EMBL:AJA44729.1,
RC   ECO:0000313|Proteomes:UP000030901};
RX   PubMed=25527542;
RA   Engel P., Vizcaino M.I., Crawford J.M.;
RT   "Gut symbionts from distinct hosts exhibit genotoxic activity via divergent
RT   colibactin biosynthetic pathways.";
RL   Appl. Environ. Microbiol. 0:0-0(2014).
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DR   EMBL; CP009056; AJA44729.1; -; Genomic_DNA.
DR   RefSeq; WP_039104344.1; NZ_QGTI01000002.1.
DR   AlphaFoldDB; A0A0A7RZK9; -.
DR   STRING; 1267021.FPB0191_00903; -.
DR   GeneID; 78459336; -.
DR   KEGG; fpp:FPB0191_00903; -.
DR   HOGENOM; CLU_009942_6_1_6; -.
DR   OrthoDB; 5734927at2; -.
DR   Proteomes; UP000030901; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 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; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AJA44729.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030901}.
FT   DOMAIN          55..570
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   573 AA;  63805 MW;  B9C9D38CD6E5767B CRC64;
     MVKNHSYAEI AYVNGYIYTA DNCNTVCEAV AITEGYIIAI GSTAQIQNLI NEQTQVIDLQ
     GKTMLPGIID AHLHPFWGGL QLSGCHLDYA SLTVEQTLKK IQHYLDNDPN KGNDDWLQVR
     GWLRQEVLPL GTDITRSDLD QLNTVRPVIL FSNDCHTLVA NSRALEKFGL NSNTPEPKDG
     KIGRFANGEL NGILEDAPAM RAFDSIPALN DMQAIEVAKR VQRELNQQGV TTAMDARSAH
     LQFKAFKTLA NEDNLTIRLL GAIEITPDDA PTLNDIPKAI DQAKNFAQLY TQQNWSPKPD
     LKISLVKFFI DGVLQAPIMT ASLLQPYRIN QGTANNVNFV ESDRLGDLYY DNAILEKLII
     EVSKAGFYPH MHTVGEGAIE TVLKHIATLR AQHPELDHIR PSLAHNELAA PHHYALFAQL
     KAIATLSFQW AAPTNEMIEQ FHHMLGEQRF NELEPSAKFI DAGAKIAFGS DWPIDPLNEW
     FDFKVAVTRK GAGKNAQRLA TDRNLTITEV LRAATIDAAY MLGQEQNIGS IEPGKFADLI
     IIDRNPFEIE PEDIENVKVI NTIIGGKLVY QQI
//
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