ID A0A0Q0MUT6_9GAMM Unreviewed; 351 AA.
AC A0A0Q0MUT6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Formimidoylglutamase {ECO:0000313|EMBL:KPZ55834.1};
DE EC=3.5.3.8 {ECO:0000313|EMBL:KPZ55834.1};
GN Name=hutG {ECO:0000313|EMBL:KPZ55834.1};
GN ORFNames=AN393_01607 {ECO:0000313|EMBL:KPZ55834.1};
OS Pseudoalteromonas sp. P1-25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1723758 {ECO:0000313|EMBL:KPZ55834.1, ECO:0000313|Proteomes:UP000050552};
RN [1] {ECO:0000313|EMBL:KPZ55834.1, ECO:0000313|Proteomes:UP000050552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-25 {ECO:0000313|EMBL:KPZ55834.1,
RC ECO:0000313|Proteomes:UP000050552};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742}.
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:KPZ55834.1}.
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DR EMBL; LKDW01000009; KPZ55834.1; -; Genomic_DNA.
DR RefSeq; WP_055017783.1; NZ_LKDW01000009.1.
DR AlphaFoldDB; A0A0Q0MUT6; -.
DR PATRIC; fig|1723758.3.peg.1639; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000050552; Unassembled WGS sequence.
DR GO; GO:0050415; F:formimidoylglutamase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd09988; Formimidoylglutamase; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR11358:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KPZ55834.1}.
FT COILED 110..137
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 351 AA; 38434 MW; 6CFC73C8AFB0148E CRC64;
MHPTLKVYDE NAVKPYCSTR TNETKTWQSV ALLDTHVNVQ QALNDAAQFG IRYVLIGVCE
DIGPRANLGR GGSHQAWPAF LQYFLNQPVN QFSAAQQVLL LGEIDVDDVM AQAQGLNNQH
TEELAQLRKL CATIDERVEA VLMLIFNAGL EPIVIGGGHN NSFGILSALS KHIGAAVNAI
NFDPHADLRP CEGRHSGNGF SYALKKNALQ QYHIIGLHEQ KNNQAIFDLI AQNQCRYHSY
QAINIRREIS LTDAVQHALA GFNNAPLGIE LDLDSISFLP ASAYTCCGFS VSDAEHYVYL
TAKHSTARYL HLCEAAPINH PAGLKAGMQS CGQIISALVN TYLQAKLVST K
//
