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Database: UniProt
Entry: A0A1H1QYX3_9PSED
LinkDB: A0A1H1QYX3_9PSED
Original site: A0A1H1QYX3_9PSED 
ID   A0A1H1QYX3_9PSED        Unreviewed;       454 AA.
AC   A0A1H1QYX3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Formimidoylglutamate deiminase {ECO:0000313|EMBL:SDS28677.1};
GN   ORFNames=SAMN05216598_1105 {ECO:0000313|EMBL:SDS28677.1};
OS   Pseudomonas asplenii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=53407 {ECO:0000313|EMBL:SDS28677.1, ECO:0000313|Proteomes:UP000199524};
RN   [1] {ECO:0000313|Proteomes:UP000199524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23835 {ECO:0000313|Proteomes:UP000199524};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; LT629777; SDS28677.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1QYX3; -.
DR   Proteomes; UP000199524; Chromosome i.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01313; Met_dep_hydrolase_E; 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; 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:UP000199524}.
FT   DOMAIN          48..428
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   454 AA;  49833 MW;  A7D6CDE4FAFBBBCA CRC64;
     MSAFFAERAL LPSGWAKNVR LEVDAAGVLA RVQADSHAED AERLGGPLLP GMPNLHSHAF
     QSAMAGLAEV AGNPNDSFWT WRDLMYRLVG KISPEQMGII ARQLYIEMLK AGYTSVAEFH
     YVHHDTNGQP YADPAELALR ISQAATDAGI GLTLLPVLYS HSGFGGQAPN EGQRRFINST
     ENYLKLQTRL QPLLAKTPAQ ALGLCFHSLR AVTPQQISEV LAASDRQCPV HIHIAEQQKE
     VDDCLSWSGK RPLQWLYDNV EVDQRWCLVH ATHADTEEVS RMARSRAIAG LCLTTEANLG
     DGIFPAVDFL AQGGRLGIGS DSHVSLSVVE ELRWLEYGQR LRDQRRNRLY RADQPMVGRT
     LFDAALDGGA QALGQAIGGL AVGKRADWLV LDGNDPYLAT AEDDGILNRW LFAGGDRQVR
     DVMVNGQWAV RGGRHAGEQE SARAFAQVLR ELLS
//
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