ID   K9DEZ8_9BURK            Unreviewed;       458 AA.
AC   K9DEZ8;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Formiminoglutamate deiminase {ECO:0000313|EMBL:EKU83279.1};
GN   ORFNames=HMPREF9710_01366 {ECO:0000313|EMBL:EKU83279.1};
OS   Massilia timonae CCUG 45783.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU83279.1, ECO:0000313|Proteomes:UP000009874};
RN   [1] {ECO:0000313|EMBL:EKU83279.1, ECO:0000313|Proteomes:UP000009874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU83279.1,
RC   ECO:0000313|Proteomes:UP000009874};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Massilia timonae CCUG 45783.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EKU83279.1}.
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DR   EMBL; AGZI01000016; EKU83279.1; -; Genomic_DNA.
DR   RefSeq; WP_005665100.1; NZ_JH992922.1.
DR   AlphaFoldDB; K9DEZ8; -.
DR   STRING; 47229.LO55_1969; -.
DR   PATRIC; fig|883126.3.peg.1381; -.
DR   eggNOG; COG0402; Bacteria.
DR   HOGENOM; CLU_012358_3_0_4; -.
DR   OrthoDB; 9796020at2; -.
DR   Proteomes; UP000009874; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR010252; HutF.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR02022; hutF; 1.
DR   PANTHER; PTHR11271:SF48; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11271; GUANINE DEAMINASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009874}.
FT   DOMAIN          48..428
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   458 AA;  49781 MW;  D03A24EDD23FCD69 CRC64;
     MTTALFARHA LLPQGWQRDV LLEWDAHGDL TRVAPGATAS PGMRQAQYVL PGMVNLHSHA
     FQRALGGLTE RAGDGPDSFW TWRDLMYRFA ARITPGQIEA IAAQLFAECL RHGYTSVCEF
     HYLQRDADGA AYARPAETAE RVAAAGQATG MGLTLLPVLY SHAGFGEKPL APAQARFRTD
     VDEVLGIVEA LGPLRGGQLE VGAAPHSLRA ATIDQIRALA GGLPPGRPLH IHIAEQQGEV
     AQCLAHAGRR PVEYLMDHVA LDARWCLVHA THLNENEVVA LASSGAVAGL CPTTEANLGD
     GLFPLAPFIE AGGRFGVGSD SHVSQSPVEE LRWLEYGQRL LHQQRNVAHT RERRDVGDYL
     WQAALQGGAL ATGRRVGLLE AGRRADLLVL DEQHPNLDGV IESEVLGRVV FCGNDNLVRD
     VLCGGRWVVQ DGRHMAQDEV AQRYRQALRD LRAVTQEV
//