ID   A0A0Q7KNJ4_9BURK        Unreviewed;       486 AA.
AC   A0A0Q7KNJ4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=N-formimino-L-glutamate deiminase {ECO:0000313|EMBL:KQX84307.1};
GN   ORFNames=ASD34_20105 {ECO:0000313|EMBL:KQX84307.1};
OS   Variovorax sp. Root473.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1736541 {ECO:0000313|EMBL:KQX84307.1, ECO:0000313|Proteomes:UP000051275};
RN   [1] {ECO:0000313|Proteomes:UP000051275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root473 {ECO:0000313|Proteomes:UP000051275};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX84307.1, ECO:0000313|Proteomes:UP000051275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root473 {ECO:0000313|EMBL:KQX84307.1,
RC   ECO:0000313|Proteomes:UP000051275};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQX84307.1}.
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DR   EMBL; LMEV01000020; KQX84307.1; -; Genomic_DNA.
DR   RefSeq; WP_056583560.1; NZ_LMEV01000020.1.
DR   AlphaFoldDB; A0A0Q7KNJ4; -.
DR   OrthoDB; 9796020at2; -.
DR   Proteomes; UP000051275; 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:UP000051275}.
FT   DOMAIN          50..458
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   REGION          72..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  52265 MW;  D24341DBCFE96643 CRC64;
     MTHTLFAADA LLPEGWTRNV LLTWNDAGQL TQVQAGAQRP ADAQAAQGPV IPGMPNLHSH
     AFQRAFAGLT EHRAEPEKAT GRPELSRPPR GEVPTLSAPG GVADSFWSWR TLMYRFAARL
     GPQHMEAIAT WLYAEMLEAG YTSVCEFQYV HHDTDGRPYT DDAALSRALL RAAQATGIGF
     TLLPVLYQTS GFGDQPPTEG QRRFIRSTES MLRLLETLKP DCDAQGARLG LAPHSLRAVP
     PDALHEALAG LDAIDRTAPV HIHIAEQTKE VDDCVEWSGL RPVEWLLDHA RVDARWCLVH
     ATHMNDAEYE YAARSGAVAG LCPTTEANLG DGIFDFAKWR SHGGAWGVGS DSHASVNAAE
     ELLMLEYSQR LAKRQRNVGA SAAQPHVATA LTLEAVQGGA QASARAVGGL AAGQQADFVV
     LDAAHVALQG LSAPDMLSAH VFASHRTSAV DAVWVAGRAR VAAGRHVLHD EAVSAFVAAR
     TRLLQD
//