ID W0B878_9GAMM Unreviewed; 572 AA.
AC W0B878;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Putative metal-dependent hydrolase with the TIM-barrel fold {ECO:0000313|EMBL:AHE66080.1};
GN ORFNames=Loa_00509 {ECO:0000313|EMBL:AHE66080.1};
OS Legionella oakridgensis ATCC 33761 = DSM 21215.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE66080.1, ECO:0000313|Proteomes:UP000018838};
RN [1] {ECO:0000313|EMBL:AHE66080.1, ECO:0000313|Proteomes:UP000018838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA Heuner K.;
RT "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT characterization reveals its replication capacity in amoebae.";
RL Int. J. Med. Microbiol. 303:514-528(2013).
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DR EMBL; CP004006; AHE66080.1; -; Genomic_DNA.
DR AlphaFoldDB; W0B878; -.
DR KEGG; lok:Loa_00509; -.
DR PATRIC; fig|1268635.3.peg.498; -.
DR eggNOG; COG1574; Bacteria.
DR HOGENOM; CLU_009942_2_0_6; -.
DR Proteomes; UP000018838; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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 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:AHE66080.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018838}.
FT DOMAIN 84..562
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 572 AA; 63840 MW; AB378E325A350185 CRC64;
MQFFLIIFTF LFIKLIYPSA LYASEIRSSA MLCRNADKIF TNATFLTMNP NQPVAKAVAV
TKERIVAIGE KKQLLNRCQG ENTKIINLKN TIVTPGFIDT YSQFVLYGWL ANHAFDVSTS
NVFQRDDWKP VKTLDQFLTT IKHQPKNRDQ WLIISGFDES KIHGGQLTTA MLDDIADNSP
VIVFSSSAEK ALLNHAAMDK IKQQDDGKTL AIEADGSVSG TSLNTLLNKL IPPNEVAEAI
KTAANRYARQ GYTTVTQVYG PNDWLPIYDE LTQNANLPVD VIYNPSTLAD KQRLDIIYKD
NPRLYPGPLL LQVDGPVQDF SAYLTRPYTQ SSPPRSIDWR GTLKQSTEGI EKTISEANKN
GLAIAIDSHG DAALDLSLNA IQKIQSVSKN HKPTPVILNM QYVREDQLTR MRQMGIKASW
FGPYLYYWGE SMCYEGLGSE RAHRSNPVAT AEKILGNTSV HAGTPSASPA PLQIMNWLIT
RKVQKWNYPV NRKCPPYFAI EERVNAQDAL QMFTIHAAEL YGIDEDKGSL ALGKLADMAI
LSGNPLNSNL ETITVLGTIT RGIVHWNEPQ DH
//
