ID F7XDT4_SINMM Unreviewed; 661 AA.
AC F7XDT4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN OrderedLocusNames=SM11_pC0636 {ECO:0000313|EMBL:AEH81709.1};
OS Sinorhizobium meliloti (strain SM11).
OG Plasmid pSmeSM11c {ECO:0000313|EMBL:AEH81709.1,
OG ECO:0000313|Proteomes:UP000009045}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH81709.1, ECO:0000313|Proteomes:UP000009045};
RN [1] {ECO:0000313|EMBL:AEH81709.1, ECO:0000313|Proteomes:UP000009045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM11 {ECO:0000313|EMBL:AEH81709.1,
RC ECO:0000313|Proteomes:UP000009045};
RC PLASMID=pSmeSM11c {ECO:0000313|Proteomes:UP000009045};
RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT isolate SM11 extends the S. meliloti pan-genome.";
RL J. Biotechnol. 155:20-33(2011).
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DR EMBL; CP001831; AEH81709.1; -; Genomic_DNA.
DR RefSeq; WP_014531373.1; NZ_JAJJBH010000005.1.
DR AlphaFoldDB; F7XDT4; -.
DR KEGG; smx:SM11_pC0636; -.
DR PATRIC; fig|707241.3.peg.4608; -.
DR HOGENOM; CLU_009942_4_3_5; -.
DR Proteomes; UP000009045; Plasmid pSmeSM11c.
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; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Plasmid {ECO:0000313|EMBL:AEH81709.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..661
FT /note="Amidohydrolase 3 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003364615"
FT DOMAIN 86..570
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 661 AA; 72929 MW; AA6DA7AE89A0EE96 CRC64;
MPTRRGFLGA ASALALPNLF SPARAADPVS TSGDKPMSAD LILHHGLVTT LDRTNPNATA
IAIRDSKFLA VGDDRDIMAL AGPETKVIDL KGKRVLPGLI DNHTHVVRGG LNYNMELRWD
GVRSLADAMD MLKRQVAITP PPQWVRAVGG FTEHQFVEKR LPTIDEINAV APDTPVFLLH
LYDRALLNGA ALRAVGYTKD TPNPPGGEII RDASGNPTGM LLAKPNAAIL YSTLAKGPKL
PFEYQVNSTR HFMRELNRLG VTGVIDAGGG YQNYPDDYAV IQKLADDGQM TVRLAYNLFT
QKPKEEKQDF LNWTSSVKYK QGDDYFRHNG AGEMLVFSAA DFEDFRQPRP DMPPEMEGDL
EEVVRVLAEN RWPWRMHATY DETISRALDV FEKVNQDMPL EGLNWFFDHA ETISERSIDR
IAALGGGIAT QHRMAYQGEY FVERYGHGAA EATPPIAKML EKGVHVSAGT DATRVASYNP
WVSLSWMITG KTLGGMQLYP RANCLDRETA LRMWTENVTW FSNEEGKKGR IEKGQFADLI
VPDKDFFACP EDEISFITSE LTMVGGKIVY GTGTFADFNE NDVPPAMPDW SPVRMFGGYA
AWGEPEGAGK RSLRRTAMAT CGCASNCNVH GHDHAGAWTS KLPISDLKGF FGALGCSCWA
V
//
