ID A0A8T8K3D2_9EURY Unreviewed; 305 AA.
AC A0A8T8K3D2;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:QUH22924.1};
DE EC=3.5.3.11 {ECO:0000313|EMBL:QUH22924.1};
GN Name=speB {ECO:0000313|EMBL:QUH22924.1};
GN ORFNames=HYG87_03635 {ECO:0000313|EMBL:QUH22924.1};
OS Methanobacterium alkalithermotolerans.
OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=2731220 {ECO:0000313|EMBL:QUH22924.1, ECO:0000313|Proteomes:UP000681041};
RN [1] {ECO:0000313|EMBL:QUH22924.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MethCAN {ECO:0000313|EMBL:QUH22924.1};
RA Postec A., Quemeneur M.;
RT "Methanobacterium. sp. MethCan genome.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR036979-1};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR036979-1};
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; CP058560; QUH22924.1; -; Genomic_DNA.
DR RefSeq; WP_211533870.1; NZ_CP058560.1.
DR AlphaFoldDB; A0A8T8K3D2; -.
DR GeneID; 64819826; -.
DR KEGG; meme:HYG87_03635; -.
DR OrthoDB; 7186at2157; -.
DR Proteomes; UP000681041; 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:0033389; P:putrescine biosynthetic process from arginine, via agmatine; IEA:TreeGrafter.
DR CDD; cd11593; Agmatinase-like_2; 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; ARGINASE/AGMATINASE; 1.
DR PANTHER; PTHR11358:SF26; GUANIDINO ACID HYDROLASE, MITOCHONDRIAL; 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 Manganese {ECO:0000256|PIRSR:PIRSR036979-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036979-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000681041}.
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 154
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
SQ SEQUENCE 305 AA; 34312 MW; 325FC7AAB202694B CRC64;
MLFYTHNPSK FAFSQDRTDF EKLIISKSKP GAKNNQKPVF ALLGVPFDGT TTYLPGTRFG
PAGVREASYN FERYNLTWNR VIDSLFFDLG NVEVIHGNFK KTCIQLQDTI SELLSRDVTP
LLIGGEHSLS YAMARALKLH NIFYEVTVVH FDAHMDMIDS YMGEKYSHAT VMRRISELNP
RRIIQLGVRS ASYEEKEFAD DKGIEYYTAA TINDDINQIK EVLSSINGPI YLTIDMDVFD
PSEAPSVGNP TPCGIKSHQM EKFMLILSKK NVVALDVVET ASDKIGDLTS VNAAKIILDF
ICLQE
//
