ID A0A2Z3HAE2_9BACT Unreviewed; 870 AA.
AC A0A2Z3HAE2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:AWM39965.1};
GN ORFNames=C1280_25130 {ECO:0000313|EMBL:AWM39965.1};
OS Gemmata obscuriglobus.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Gemmata.
OX NCBI_TaxID=114 {ECO:0000313|EMBL:AWM39965.1, ECO:0000313|Proteomes:UP000245802};
RN [1] {ECO:0000313|EMBL:AWM39965.1, ECO:0000313|Proteomes:UP000245802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5831 {ECO:0000313|EMBL:AWM39965.1,
RC ECO:0000313|Proteomes:UP000245802};
RA Franke J., Blomberg W., Selmecki A.;
RT "G. obscuriglobus.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP025958; AWM39965.1; -; Genomic_DNA.
DR RefSeq; WP_010034629.1; NZ_CP042911.1.
DR AlphaFoldDB; A0A2Z3HAE2; -.
DR KEGG; gog:C1280_25130; -.
DR OrthoDB; 9802793at2; -.
DR Proteomes; UP000245802; Chromosome.
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:AWM39965.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245802};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..870
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016247149"
FT DOMAIN 89..421
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 732..840
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 437..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 91418 MW; 6A54B23BEBD9C903 CRC64;
MRRLAALVPI VIALSLPLVP GAGAPAAARA ADADRVTAFT GATIHTAATD RPIENGTLVV
KGGRIAAVGA AADVTVPPGA EVVDLKGRVV IPGLVDTHSH VGVYSRPGVA ANSDGNEMSG
PVQPGVRAID SFNADDPGIK MALAGGVTTA NVMPGSGNVI GGQTVYVKYR GRSVEEMRVT
GRAWGKEILG GLKMANGENP KGYGRGKGVA PFTRMKVAAM QRETFQKAKE YRAKLEGGGK
VDRDVALEPL VEVLDGKRTV HFHCHRADDL LTAVRLSEEF GFELVLQHAT EGYRVADVLA
KKKIPVSLTL IDSPGGKAET MGLLEENAAI LNSAGVIVTI NTDDSVTESR FLLRTGAIAA
RGGMSEADAL KAITIRAAKL LHLDHRLGSL EKGKDADFAV LSGSPFSVYT RVEQTWIDGQ
KVFDVIPDRG YQTGGFALPA GEKLPTPPPG PRPAPEARDL GTPTFDGNTP ELKGAVAVTA
EFIHTGGRVF PGVIVAKDGK ILHVVAGEAT AKNMPIYKAK HVTPGLIDPF CSAGLSGAWN
SPADQDQDET SDPNQADLRA LDGFNPREPL LDFLVANGTT VVHATPGRVN PIAGRGGVFR
ADGTTADSAL VPVGALVVNL GESSKGKSPT TRMGVAALVR KAFTDADAYR TSKPAAKNPK
HEALVPALEG KANVYFAAHR RDDIQTALRI AAEFKLKPVI ALGTEGYRMA EELKQAGVPV
VVHPTMLRAG GSIETMHAFT GNVAALDAAG VPVTVCTGFE GYVPKTRVLR YEAAMAAAAG
MDRERALSAI TINAAKLLGI DKEYGSIEVS KVADLVLYDG DPFEHTTHVT HTLLRGKVAY
DRAEYLKLPF ERRVLPLLTG GSGTGCCLGW
//
