ID L1KSP1_9ACTN Unreviewed; 361 AA.
AC L1KSP1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:EKX63786.1};
DE EC=3.5.3.11 {ECO:0000313|EMBL:EKX63786.1};
GN Name=speB {ECO:0000313|EMBL:EKX63786.1};
GN ORFNames=STRIP9103_03307 {ECO:0000313|EMBL:EKX63786.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX63786.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX63786.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX63786.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:EKX63786.1}.
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DR EMBL; AEJC01000409; EKX63786.1; -; Genomic_DNA.
DR AlphaFoldDB; L1KSP1; -.
DR PATRIC; fig|698759.3.peg.5559; -.
DR Proteomes; UP000010411; Unassembled WGS sequence.
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 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:UP000010411}.
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 38976 MW; 796D9612E233ECC1 CRC64;
MRRARSKSEF PESYKKQYIR DEAQERRHTS MSSNETPLVG APRGPVDSSR IPRYAGPATF
ARLPRLDEVG RADVAVVGVP FDSGVSYRPG ARFGGNAIRE ASRLLRPYNP AQDASPFALA
QVADAGDIAA NPFDIDEAVE TVEAAADELL ATGARLMTLG GDHTIALPLL RSVAKKHGPV
ALLHFDAHLD TWDTYFGAEY THGTPFRRAV EEGILDTSAL SHVGTRGPLY GKRDLDDDAK
MGFGVVTSAD VMRRGVDEIA DQLRQRVGDR PLYISIDIDC LDPAHAPGTG TPEAGGMTSR
ELLEILRGLA GCNLVSADVV EVAPAYDHAE ITAVAASHTA YELTTIMTRR IAEARKENEG
K
//
