ID B3QEJ0_RHOPT Unreviewed; 626 AA.
AC B3QEJ0;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:ACF00906.1};
GN OrderedLocusNames=Rpal_2392 {ECO:0000313|EMBL:ACF00906.1};
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=395960 {ECO:0000313|EMBL:ACF00906.1, ECO:0000313|Proteomes:UP000001725};
RN [1] {ECO:0000313|EMBL:ACF00906.1, ECO:0000313|Proteomes:UP000001725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1 {ECO:0000313|EMBL:ACF00906.1,
RC ECO:0000313|Proteomes:UP000001725};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001096; ACF00906.1; -; Genomic_DNA.
DR RefSeq; WP_012495664.1; NC_011004.1.
DR AlphaFoldDB; B3QEJ0; -.
DR KEGG; rpt:Rpal_2392; -.
DR HOGENOM; CLU_009942_4_3_5; -.
DR OrthoDB; 9811399at2; -.
DR Proteomes; UP000001725; 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:SF23; AMIDOHYDROLASE YTCJ-RELATED; 1.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 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:ACF00906.1}.
FT DOMAIN 52..536
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 626 AA; 68750 MW; 1F42A1CC45CD66CB CRC64;
MTDAPDLILH RGLFTTLDRS NPTVSAVAIS GGRFSAVGHD REVLPLAGPS TKVIDLKGRR
VLPGLIDNHL HIIRGGLNFN MELRWDGVRS LADAMNMLKR QVAITPPPQW VRVVGGFTEH
QFAEKRLPTI EELNAVAPDT PVFLLHLYDR AILNGAALRA VGYTKDTPEP PGGEITRDAN
GNPTGLLLAK PNANILYATL AKGPKLPFDY QVNSTRHFMR ELNRLGVTGA IDAGGGFQNY
PDDYAVIQKL DEEGLLTIRL AYNLFTQKPK GEKDDFLNWT KTSKYKQGND YFRHNGAGEM
LVFSAADFED FRVPRPDMPP EMEGELEEVV RILVQNKWPW RLHATYDETI SRALDVFEKV
NQDTPLDGLH WFFDHAETIS DRSIDRIAAL GGGIAVQHRM AYQGEYFVER YGFGAAEATP
PVKRILDSGV KVSAGTDATR VASYNPWVSL SWLVTGRTVG GLRITPQRNC LDRETALRMW
TENVTWFSNE EGNKGRVAVG QLADVVVPDR DYFSCSEAEI ADTTSLLTMV GGKVVYGAGE
FAGLDDSAPP PAMPDWSPVR RFGGYAAWAD DESAAGKVAG QAMSSCGCAN SCTLHGHDHA
TAWSSKLPVS DLKSFWGALG CACWAV
//
