ID A0A101ABZ0_9MYCO Unreviewed; 323 AA.
AC A0A101ABZ0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:KUI19989.1};
GN ORFNames=AU194_03570 {ECO:0000313|EMBL:KUI19989.1};
OS Mycobacterium sp. GA-2829.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1772283 {ECO:0000313|EMBL:KUI19989.1, ECO:0000313|Proteomes:UP000053444};
RN [1] {ECO:0000313|EMBL:KUI19989.1, ECO:0000313|Proteomes:UP000053444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA-2829 {ECO:0000313|EMBL:KUI19989.1,
RC ECO:0000313|Proteomes:UP000053444};
RG TB Trials Study Group;
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E.L., Macaden R.,
RA Grewal H.M.S.;
RL Submitted (JAN-2016) 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:KUI19989.1}.
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DR EMBL; LQIT01000089; KUI19989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101ABZ0; -.
DR STRING; 1772283.AU194_03570; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000053444; 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 Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053444}.
SQ SEQUENCE 323 AA; 34864 MW; 33A24952661F411E CRC64;
MNNDRALSAG RTIVGPADPQ VQPRYAGWTT FARLPRLEDV EHADVVVVGV PFDSAVTYRP
GARFGPNAIR QGSRLIRGYN PELDIKPFEV CQFADAGDLA CNPFDIGEAV NQVADQLTEL
LAGGTRAVIL GGDHSVALPS LRAAHSVHGP MALVHFDAHL DTWDRYYGAD ITHGSPFRRA
FEEGLLLDRN MHVGVRGSIY DKQDLVEDAN FGFSVITCRD IDSLGAEGIV EKIRARVGDA
PVYVSVDIDV LDPAHAPGTG TPEAGGMSSR ELLEVIRGLD KVNLVAVDVV EVSPAYDHAE
ITAIAAANVT WEFLSVFGRK AQR
//