ID A0A0K8QMW6_9GAMM Unreviewed; 1054 AA.
AC A0A0K8QMW6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:GAP66071.1};
GN ORFNames=MBSD_n1373 {ECO:0000313|EMBL:GAP66071.1};
OS Mizugakiibacter sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Mizugakiibacter.
OX NCBI_TaxID=1475481 {ECO:0000313|EMBL:GAP66071.1};
RN [1] {ECO:0000313|EMBL:GAP66071.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SkMP5 {ECO:0000313|EMBL:GAP66071.1};
RA Rikkerink E.H.A., Fineran P.C.;
RT "Complete DNA Sequence of Pseudomonas syringae pv. actinidiae, the Causal
RT Agent of Kiwifruit Canker Disease.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF970187; GAP66071.1; -; Genomic_DNA.
DR RefSeq; WP_062536417.1; NZ_DF970187.1.
DR AlphaFoldDB; A0A0K8QMW6; -.
DR STRING; 1475481.GCA_000953855_01392; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000253740; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01309; Met_dep_hydrolase_C; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:GAP66071.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253740};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1054
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005514921"
FT DOMAIN 395..455
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 883..971
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 115..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1054 AA; 112810 MW; A2E484AB16367D7D CRC64;
MSNTRYRPRR HTLPSCLAAL ALTLLAGAPL HAQVDTRPVE GIADRTPRLA AFVHARLVIK
PGEVVDDGTL VVRDGVIVAA GRGVKIPDGA ARIDLGGKTV FAGFIDPLSA YAQPVPPETP
AAGGGRRGAS PAMPQPQPGA AYWNARVHPQ EDVAASVKPD AKAAEKLRAL GFTDALSVPQ
RGVFRGQSAL YALSDAANGN DALIRARVAQ HLAFETSGWG SAEYPGSLMG AIALIRQALY
DARWQQQRLA WQAKRAEAER TAPNDALAAL APLLAGRQPA IFATRDELDY GRALAIAREF
GLKPVLAGNG HEYRMAPKLA AAGVPVIVPL DFPEAPAVED PDAALDVSLA ELEHWRWAPY
NARVLAEAGV PFAFTAAGLK KPEEEFWKRV RKTVADGLDP DAALAALTTQ PAAMLGVADE
LGTLQPGRLA HFVVADADLL YRDDARIYET WIDGRRYRLA DPAAPDPRGG WTLAWSGGNG
PASMEVSGKD AALTAKAGGE SFPLTQSDDG RLLLYVPGKL LGSARERVVV VAQLDGGAFD
GRAELEDGRR LRVHGTLTQP APRALAAAPA KPPLPGELRF PAGAYGRRGL PPQPAALVVR
HATIWTQGPL GVLEDADLLV EKGKVAAVGR NLKAPSGAVE IDGSGKHVSP GIIDAHSHIA
VSGGVNEATH AVTSEVRIGD VLDPTDIIIY RQLAGGTTTA MVLHGSANPI GGQSQIVKLR
WGADADGLKF KRAPETIKFA LGENVKQSNW GDNFTTRYPQ TRMGVEQIDL DSLLAAQAYG
AALNAGHAAD GGPLRRDLRL EALWEVLQGK RLVQIHSYRQ DEILGFIRIA QQFHIVPTFQ
HVLEGYKVAD AIARLGAGAS TFSDWWAYKF EVRDAIPYNG ALMTRQGVTV SFNSDDDEMG
RRLNTEAAKS VKYGGLSDTE ALALVTINPA RQLHIDKYVG SLEPGKDADF VIWNAPPLST
LAVPQQTWVD GRKYFDRADD LAERANVERE RAALIAAALP ERVKALAQDG DKKDKAGAAA
PQPREEDLLR RYAARRPIYH DDEPVNGCTD AESH
//
