ID I3YX13_AEQSU Unreviewed; 559 AA.
AC I3YX13;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative TIM-barrel fold metal-dependent hydrolase {ECO:0000313|EMBL:AFL81531.1};
GN OrderedLocusNames=Aeqsu_2066 {ECO:0000313|EMBL:AFL81531.1};
OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL81531.1, ECO:0000313|Proteomes:UP000006049};
RN [1] {ECO:0000313|EMBL:AFL81531.1, ECO:0000313|Proteomes:UP000006049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC {ECO:0000313|Proteomes:UP000006049};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Aequorivita sublithincola DSM 14238.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003280; AFL81531.1; -; Genomic_DNA.
DR AlphaFoldDB; I3YX13; -.
DR STRING; 746697.Aeqsu_2066; -.
DR KEGG; asl:Aeqsu_2066; -.
DR eggNOG; COG1574; Bacteria.
DR HOGENOM; CLU_009942_1_0_10; -.
DR Proteomes; UP000006049; 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:AFL81531.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..559
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003683130"
FT DOMAIN 83..556
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 559 AA; 62142 MW; EB46226EBC433486 CRC64;
MADVFYFYTS TKPIMKKLLF LLLAISIASC APEKLPADLL IKNATIYTVD KDFSTANALV
VKDGKILEIG LKPELELKYT IKETYDAKGN TVVPGLIDAH AHLYGLGLGL QNVDLVGTTS
FDEILGRVVA FQEEKNMPYI IGRGWDQNDW DDKNFPTKKE LDSLFPDTAV SLRRIDGHAM
LVNSKALELA GITSKTKVAG GEIVLENGEP SGIIIDAPMD LIAKTFPEIT SEVSTEALLE
AEKIALSYGL TTVDDAGLNR NIIELIDALQ KEGKFKLRIY AMVSNSPENL DYYLKQGIQK
TDRLSVRSFK VYADGALGSR GAAMRESYSD MQLHFGAMIT TADSLNYLAE KIAASEFQMN
THAIGDSANI AVLRAYKKAL EGKTDRRWRV EHAQIISEPD FNYFDDNNNI LPSVQPTHAT
SDMYWAEDRV GAERMKGAYA YKKLLDEAGM VALGTDFPVE HVNPMYTFYA AVARKDLKNY
PEDGFQMKDA LTREEALKGM TIWAAFANFE ENEKGSIEVG KFADFTILDK DIMKVDEKEL
SNTKVIATFI NGEMVYNAQ
//
