ID V4PFR7_9CAUL Unreviewed; 590 AA.
AC V4PFR7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=AEAC466_10360 {ECO:0000313|EMBL:ESQ84140.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ84140.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ84140.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ84140.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESQ84140.1}.
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DR EMBL; AWGE01000008; ESQ84140.1; -; Genomic_DNA.
DR RefSeq; WP_023458081.1; NZ_AWGE01000008.1.
DR AlphaFoldDB; V4PFR7; -.
DR STRING; 1282362.AEAC466_10360; -.
DR PATRIC; fig|1282362.3.peg.2049; -.
DR eggNOG; COG1574; Bacteria.
DR OrthoDB; 9811399at2; -.
DR Proteomes; UP000017826; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000017826};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..590
FT /note="Amidohydrolase 3 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004724634"
FT DOMAIN 79..586
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 193..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 63201 MW; 15B2BBF2AE574DD3 CRC64;
MKASRFALLA FAGLAPALLA LALPAQAKPQ KADTVFLHGY VYTVDAADSV AEAVAVRDGQ
IVYVGGDDGA RALIGKATRV VDLSGRLLMP GLIDGHMHPQ AGGLRMLGCN LDYAALTQAE
FQARIQKCVD DDKTAGPDDW LIVINWFEQG AKPEGTVMTR AALDAVRTTR PIKVHSSFGH
SDLTNTRGLK LAGITRDTPD PKDGTIVRDA SGEPTGLLQE AAQDLIDKLI PAPSVEMNYK
ATQLALKAMR EQGITSFLDA YTDIETLTAY STVVREGGLT ARGHFAVLID SPEGYDAGKA
VAEVLRQKAE FDRPGVGPAP GMTVDTAKLF LDGVYSAPAY SAMMIQPYFE HGRPGHNRGP
KPFFTDDQLQ DTLIRLAAVG LNPHMHAEGD GSVRQGLNAV AAMRKVHPGS DIRPAIAHDE
IVHPDDFSRF AEVGALPVLS FQWERPSVDI EQSKPALGPV RAALMEPAAL LDINGARIVY
GSDWPVDALN EWLALQIAVT RTAIGDDAVK YPGRLGIDPG LSVAQAVRAI TLNAAYSLRQ
EDQTGSVEVG KLADLIVLDR NLFKIKPEEI GGTQVLLTMV GGKVVYQTLK
//
