ID Q1IRQ7_KORVE Unreviewed; 583 AA.
AC Q1IRQ7;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:ABF40443.1};
GN OrderedLocusNames=Acid345_1441 {ECO:0000313|EMBL:ABF40443.1};
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Koribacter.
OX NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF40443.1, ECO:0000313|Proteomes:UP000002432};
RN [1] {ECO:0000313|EMBL:ABF40443.1, ECO:0000313|Proteomes:UP000002432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345 {ECO:0000313|EMBL:ABF40443.1,
RC ECO:0000313|Proteomes:UP000002432};
RX PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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DR EMBL; CP000360; ABF40443.1; -; Genomic_DNA.
DR RefSeq; WP_011522245.1; NC_008009.1.
DR AlphaFoldDB; Q1IRQ7; -.
DR STRING; 204669.Acid345_1441; -.
DR EnsemblBacteria; ABF40443; ABF40443; Acid345_1441.
DR KEGG; aba:Acid345_1441; -.
DR eggNOG; COG1574; Bacteria.
DR HOGENOM; CLU_009942_1_0_0; -.
DR OrthoDB; 9767366at2; -.
DR Proteomes; UP000002432; 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 Reference proteome {ECO:0000313|Proteomes:UP000002432};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..583
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004191512"
FT DOMAIN 97..580
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 46..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 64272 MW; A53305290AFEDD8D CRC64;
MKRELLAVLL TATALMAADK KENKSAPQEA DAIYYNANVY VAPSKAAAET QSTHDENTAK
PSSPAPRPRA FAVKDGKFLA IGTDKEIWIY KGKKTTLVDL KGQFVMPGFN DAHVHLGDGG
REMLNVELAG TKSLDEMKQR IAERVKSAAP GEWILGGGWD QTKWTENKLP TRKDLDAVTA
GHPAFFDRAD GHIAVANSAA ITAAKVDKST TAPAGGAIDH DAKGEPTGIF REGAKGLISS
IIPPPTPTQR RKGIELALED AAQHGITSLQ DNSPWEDFLV YEELESEGKL TARIAEWLPF
TAELNTLDQH RSHHPGSDPM LHTTMLKGFM DGSLGSRTAA LQRPYEDDPT NKGLPQFDQE
TLNKLADERI AAGYQLGFHA IGDEGVQMAL DAFAEAQRYL RDHNQNGRDL HDLRFRIEHS
QVLSSDQFQR YKELGVIASM QPNHLLTDMN WALDRLGTAR ARYSYAWRDF LDAGVPLAFG
TDYPVEPITP FRGLYAAVTR QNEAMNREFF PVQKITIDEA IAAYTEGAAY AQFEESLKGR
IAPGMYADFV VLDRDITDIR PHDILGTQVL RTVVGGKTVY EVE
//
