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
//