ID Q12QP0_SHEDO Unreviewed; 619 AA.
AC Q12QP0;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:ABE54236.1};
GN OrderedLocusNames=Sden_0948 {ECO:0000313|EMBL:ABE54236.1};
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE54236.1, ECO:0000313|Proteomes:UP000001982};
RN [1] {ECO:0000313|EMBL:ABE54236.1, ECO:0000313|Proteomes:UP000001982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC {ECO:0000313|Proteomes:UP000001982};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000302; ABE54236.1; -; Genomic_DNA.
DR AlphaFoldDB; Q12QP0; -.
DR STRING; 318161.Sden_0948; -.
DR KEGG; sdn:Sden_0948; -.
DR eggNOG; COG1574; Bacteria.
DR HOGENOM; CLU_009942_6_1_6; -.
DR Proteomes; UP000001982; 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:ABE54236.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001982}.
FT DOMAIN 121..601
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 619 AA; 67245 MW; 71558AB58D28BEFE CRC64;
MTMTMTMTNT ASRSLGQKYR RSLLKPFVSL VVGAAAPLAL LLSPALMAHT SLVSNIQGYS
MAAGKLSRFN AILFTDDKID ALYGHDFPAA PESFEHLLNE KHHVDDLSHS SRIDNNKVNH
IDGQGLTLLP GLIDAHGHVL GYGLSLLQAQ LRDSQSEQDA VAKVQTFRKA HPQLTWVQGR
GWNQVLWPSK AFPSKDLLDK AFPDTPVWLI RIDGHAGWAN SAAMKLANIS VDTQAPEGGE
IIRDSQGQAT GVFIDNAMGL IAANIPPLTL DEQKAVLLSS LQQLATLGLT SVHDAGIGST
TIKAYKELDQ AKHLPIRVYA MIDATDEHFS DLIKAGPTLS DLGHSDMLAI NSVKISADGA
LGSRGAALIS DYSDKAGHKG LLLYPEAKLT QTMEAAMAAG FQVNTHAIGD EANKQVLDNY
QALIAKTKTK ALRHRVEHAQ VLQLADIPRF SALGVIASMQ ATHATSDKNM AEDRLGPDRI
KGAYAWQKLI KSGAIIAAGS DFPIESPNPF FGLHASVTRQ DQQNQPLGGW HSIERMSLAQ
AFETFSYNAA FAAHQEQIIG SLAPGMKADF ILIDKNIFTL APELIWQTQV QQTWVNGRRL
YQTHADLKMS ETQHTHPAN
//
