ID Q2K9W6_RHIEC Unreviewed; 342 AA.
AC Q2K9W6;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Agmatinase protein {ECO:0000313|EMBL:ABC90370.1};
DE EC=3.5.3.11 {ECO:0000313|EMBL:ABC90370.1};
GN Name=speB1 {ECO:0000313|EMBL:ABC90370.1};
GN OrderedLocusNames=RHE_CH01568 {ECO:0000313|EMBL:ABC90370.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC90370.1, ECO:0000313|Proteomes:UP000001936};
RN [1] {ECO:0000313|EMBL:ABC90370.1, ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; CP000133; ABC90370.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2K9W6; -.
DR KEGG; ret:RHE_CH01568; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_039478_0_0_5; -.
DR Proteomes; UP000001936; Chromosome.
DR GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-EC.
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 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:UP000001936}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 36865 MW; 5BE7A654EAD5BCE6 CRC64;
MASRYKVDIE RDHASADREG APLANKTIDH AFTATTLTSA ASDPTFAGAL SFMRRRFTKE
LAGVDVAVWG IPFDAATSNR PGTRFGPQAI RRASAIFDND AQYPFNRDLF ADMAVIDYGD
CLLDYGNHQD TPGAIERQAN AILDSGAFLL TLGGDHYVTW PLLKAHAAKH GPLALVQFDA
HQDTWFDEER RIDHGSFVAR AVREGIVDPD RSIQIGIRTH APEDCGINIL YGHQVEDMNA
GDIASAIISH TRGAPAYLTF DIDCLDPAFA PGTGTPVAGG PSSAKILSVL QRLHQLDIRG
ADVVEVSPPY DHADVTAIAG ATVAMYMLGL RAERRAIAVS QG
//
