ID A0A1V9KD40_9ACTN Unreviewed; 313 AA.
AC A0A1V9KD40;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:OQQ17510.1};
GN ORFNames=B0675_10620 {ECO:0000313|EMBL:OQQ17510.1};
OS Streptomyces sp. M41(2017).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1955065 {ECO:0000313|EMBL:OQQ17510.1, ECO:0000313|Proteomes:UP000192467};
RN [1] {ECO:0000313|EMBL:OQQ17510.1, ECO:0000313|Proteomes:UP000192467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:OQQ17510.1,
RC ECO:0000313|Proteomes:UP000192467};
RX PubMed=28326787; DOI=10.1021/acs.orglett.7b00545;
RA Wyche T.P., Ruzzini A.C., Beemelmanns C., Kim K.H., Klassen J.L., Cao S.,
RA Poulsen M., Bugni T.S., Currie C.R., Clardy J.;
RT "Linear Peptides Are the Major Products of a Biosynthetic Pathway That
RT Encodes for Cyclic Depsipeptides.";
RL Org. Lett. 19:1772-1775(2017).
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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:OQQ17510.1}.
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DR EMBL; MWFK01000001; OQQ17510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9KD40; -.
DR STRING; 1955065.B0675_10620; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000192467; Unassembled WGS sequence.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd11592; Agmatinase_PAH; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR NCBIfam; TIGR01230; agmatinase; 1.
DR PANTHER; PTHR11358:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000192467}.
SQ SEQUENCE 313 AA; 33451 MW; E7567AAF56EFC690 CRC64;
MERIDSHVSP RYAQIPTFMR LPHDQNPRGY DVVVIGAPYD GGTSYRPGAR FGPRAIRNES
GLIHGVGIDR GPGTFDLINC VDGGDIDLTP FNMNIAIETA QRHLAELLKS NAAFMMLGGD
HSLTVAALRA VAEQHGPVAV LHLDAHSDTN PAFYGGQYHH GTPFRHGIEE KLIDPAAMVQ
IGIRGHNPKP DSLDYARGNG VRVVTADEFG DLGVAGTADL VRERVGGRPV YVSVDIDVVD
PAFAPGTGTP APGGLSSREL LALLRCVGDL RPVGFDVMEV SPLYDHAGIT SVLATEIGAE
LLYQYARAHR APA
//