ID Q2JMJ7_SYNJB Unreviewed; 456 AA.
AC Q2JMJ7;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Amidohydrolase family protein {ECO:0000313|EMBL:ABD02040.1};
DE EC=3.5.4.1 {ECO:0000313|EMBL:ABD02040.1};
GN OrderedLocusNames=CYB_1063 {ECO:0000313|EMBL:ABD02040.1};
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD02040.1, ECO:0000313|Proteomes:UP000001938};
RN [1] {ECO:0000313|EMBL:ABD02040.1, ECO:0000313|Proteomes:UP000001938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938};
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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DR EMBL; CP000240; ABD02040.1; -; Genomic_DNA.
DR RefSeq; WP_011432694.1; NC_007776.1.
DR AlphaFoldDB; Q2JMJ7; -.
DR STRING; 321332.CYB_1063; -.
DR KEGG; cyb:CYB_1063; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_031758_5_1_3; -.
DR OrthoDB; 9815027at2; -.
DR Proteomes; UP000001938; Chromosome.
DR GO; GO:0102480; F:5-fluorocytosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004131; F:cytosine deaminase activity; IEA:UniProtKB-EC.
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:ABD02040.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001938}.
FT DOMAIN 207..418
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 456 AA; 50113 MW; 86C46BE92C15C827 CRC64;
MQIPGVAHYW LLNAQVPLSV LKEAVPGAVP NRDNLVLLDL EIEGGQIRQI QAATGIPPQG
IPSVDLRRGQ VWPCFVDIHT HLDKGHVWPR TPNPDGTFAG ARQAGQEDWV KMKQAYDGDP
EQFREDLYRR FSFGLRCSYA HGSQAVRTHL VCENPQVMGA SWEVFVQLRR EWAGKLELQA
VTLLSLDAFL TPAAEKLADK VAEVGGILGG VAAMGPELDR QLDRVFALAK ERGLALDFHT
DETDDPGSLT LRHVAAAALR NDFPHQVVCG HCCSLAVQPP EVAHKTMALV REAGIAVVSL
PMCNLYLQAR NPGHTPRWRG VTLLHELKAL GVPVMIASDN CRDPFYGFGD HDGLEVFREA
TRILHLDTPY GDWPQAITTT PARIMGLTER GQIGVGLPAD LVLFKGRGFD ELLSRPQHDR
VVLRQGQAID TTLPDYSELD DLMERVGAAV SSGSKQ
//
