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Database: UniProt
Entry: Q2RQL0_RHORT
LinkDB: Q2RQL0_RHORT
Original site: Q2RQL0_RHORT 
ID   Q2RQL0_RHORT            Unreviewed;       440 AA.
AC   Q2RQL0;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=N-isopropylammelide isopropylaminohydrolase {ECO:0000313|EMBL:ABC23585.1};
DE            EC=3.5.99.4 {ECO:0000313|EMBL:ABC23585.1};
GN   OrderedLocusNames=Rru_A2788 {ECO:0000313|EMBL:ABC23585.1};
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC23585.1, ECO:0000313|Proteomes:UP000001929};
RN   [1] {ECO:0000313|EMBL:ABC23585.1, ECO:0000313|Proteomes:UP000001929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC   {ECO:0000313|Proteomes:UP000001929};
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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DR   EMBL; CP000230; ABC23585.1; -; Genomic_DNA.
DR   RefSeq; WP_011390598.1; NC_007643.1.
DR   RefSeq; YP_427872.1; NC_007643.1.
DR   AlphaFoldDB; Q2RQL0; -.
DR   STRING; 269796.Rru_A2788; -.
DR   EnsemblBacteria; ABC23585; ABC23585; Rru_A2788.
DR   KEGG; rru:Rru_A2788; -.
DR   PATRIC; fig|269796.9.peg.2894; -.
DR   eggNOG; COG0402; Bacteria.
DR   HOGENOM; CLU_031758_0_1_5; -.
DR   PhylomeDB; Q2RQL0; -.
DR   Proteomes; UP000001929; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01293; Bact_CD; 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   PANTHER; PTHR32027; CYTOSINE DEAMINASE; 1.
DR   PANTHER; PTHR32027:SF0; CYTOSINE DEAMINASE; 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:ABC23585.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001929}.
FT   DOMAIN          48..407
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          419..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  47118 MW;  F72520041EEB09EA CRC64;
     MTTFPPAQDL IVRNASLPDG RRAQDILILA GTIKAIGPAL DAPEATPVLD AKGDLVAPPF
     VDAHFHMDSA LSYGLPRINA SGTLLEGIAL WGELKPELTH QAIVDRALAY CDWAIGRGLL
     AIRSHVDICD PRLLAVDALL EVREKVAPWL TLQLVAFPQD GFLRAQGSRE RLIAALDRGV
     DVVGGIPHFE RTMAQGAESV RALCEIAAER GLRVDMHCDE SDDPMSRHVE TLAAETTRLG
     LEGRVTGSHL TSMHSMDSYY VSKLIALMAE AELGVIANPL INITLQGRHD GYPKRRGMTR
     VPELLAAGLT VAFGHDCVMD PWYGLGSADM LEVAAMGLHV AQMTGQSAMA ECFAAVTTAP
     AKLMGLDDYG LMPGCRGDLV LLQAGDPVEA LRLRATRLAV VRGGRIIART PAATATLDLG
     DGDRPTLNPV SWRGGERPGF
//
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