ID W1RQF5_9SPHN Unreviewed; 550 AA.
AC W1RQF5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ETI59072.1};
GN ORFNames=C100_21700 {ECO:0000313|EMBL:ETI59072.1};
OS Sphingobium sp. C100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1207055 {ECO:0000313|EMBL:ETI59072.1, ECO:0000313|Proteomes:UP000018867};
RN [1] {ECO:0000313|EMBL:ETI59072.1, ECO:0000313|Proteomes:UP000018867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C100 {ECO:0000313|EMBL:ETI59072.1,
RC ECO:0000313|Proteomes:UP000018867};
RX PubMed=24482512;
RA Dong C., Bai X., Lai Q., Xie Y., Chen X., Shao Z.;
RT "Draft Genome Sequence of Sphingobium sp. Strain C100, a Polycyclic
RT Aromatic Hydrocarbon-Degrading Bacterium from the Deep-Sea Sediment of the
RT Arctic Ocean.";
RL Genome Announc. 2:0-0(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETI59072.1}.
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DR EMBL; AYOY01000200; ETI59072.1; -; Genomic_DNA.
DR AlphaFoldDB; W1RQF5; -.
DR STRING; 1207055.C100_21700; -.
DR PATRIC; fig|1207055.3.peg.4156; -.
DR eggNOG; COG3653; Bacteria.
DR Proteomes; UP000018867; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 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; IPR023100; D-aminoacylase_insert_dom_sf.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF07969; Amidohydro_3; 2.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ETI59072.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018867};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..550
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004809486"
FT DOMAIN 82..235
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 416..516
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 550 AA; 58137 MW; ABA2F97306DFA71B CRC64;
MLMPHLSASS RFRQTLRTLL LASSLAACAS AGGAAPSEQA DVLIKGGTIY DGGTGKPYVG
DVALKGDRIV YAGRTAPMTA ARVIDAKGMI VAPGFIDAHT HADSFIRSAD PAMRVNAAWL
DQGVSTVVIG VDGYGTPDVA EDAAKLQASG IGTNIIPFVG FGAVRQRVLG QDARAPDAAE
LDAMKALVAK GMCEGATGFS AGLFYAPQSF AKTDEVVAVA REAAIRGGLY DTHQRDESSY
TIGLLGSVNE AIDIGKQAGM PVHFAHIKAL GVDVQGQASA VIAQINAARA AGQDVTADQY
PWLASGSSLD ASLLPGWAVD GGGPALLRRL DDPATLARIR DEMQNNLRRR GGPKALLLIA
QDFPWTGKTL AQVAAQWQLD PRDAALRIIR QSLEATEPAK KGKGTAVASF NMAQADVDLF
MQQPWMVTSS DGSDGHPRMF ATFPEKYVRY VRDRKVIDLQ TFVRQSTGRT ADIYRIDHRG
YLKPGYYADV VVIDPAHYAP RADYIHPREL SVGVSSLFVN GALAVSDSQA TGATAGRALL
RATPAACSTD
//
