ID Q98J79_RHILO Unreviewed; 415 AA.
AC Q98J79;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Cytosine deaminase {ECO:0000313|EMBL:BAB49287.1};
GN OrderedLocusNames=mll2061 {ECO:0000313|EMBL:BAB49287.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB49287.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB49287.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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DR EMBL; BA000012; BAB49287.1; -; Genomic_DNA.
DR AlphaFoldDB; Q98J79; -.
DR KEGG; mlo:mll2061; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_031758_4_2_5; -.
DR Proteomes; UP000000552; 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:SF9; BLL3847 PROTEIN; 1.
DR PANTHER; PTHR32027; 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;
FT DOMAIN 55..402
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 415 AA; 43683 MW; 5AE470C77971EAAD CRC64;
MSEQAILSEQ TIFRNAKLAD GSLADLFVTG GRFRAIAPAG KAPPADFAAI DPADIDLSGQ
LVVPAFVEGH IHLDTSFYGD AWRPHIPCTN GFDVRERVAF QARNLAAAAP MAERAKNQLE
LCVGNGSLAM RSHVMVDASV GLRHVETILA VREKYRDLID IQLVAFPQSG ILSSPGTAEL
LDEALKLGCD LIGGLDPASF DRDVNGHLDV VFALAQKHGA GVDIHLHDGG ALGLFQVEEI
AARTKALGMA GHVAVSHAYG LGDIPADALA KAGAMLAAAG VAIMTNAPGN HAFPPVAALR
QAGVTVFSGS DNIRDSWWPY GDGDMLNRAN MIGYRSGFYE DRELEAAFDV VTHAGARALG
LADYGIAVGA SADFVAMPAQ HVPEAVVAVP KDRTVYRRGK AVARVGKMLG VSTSY
//
