ID A0A7D4CQ35_9BACL Unreviewed; 290 AA.
AC A0A7D4CQ35;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 08-OCT-2025, entry version 18.
DE RecName: Full=Agmatinase {ECO:0000256|ARBA:ARBA00067513};
DE EC=3.5.3.11 {ECO:0000256|ARBA:ARBA00066392};
DE AltName: Full=Agmatine ureohydrolase {ECO:0000256|ARBA:ARBA00082423};
GN Name=speB {ECO:0000313|EMBL:QKG85778.1};
GN ORFNames=GXN76_15830 {ECO:0000313|EMBL:QKG85778.1};
OS Kroppenstedtia pulmonis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
OC Thermoactinomycetaceae; Kroppenstedtia.
OX NCBI_TaxID=1380685 {ECO:0000313|EMBL:QKG85778.1, ECO:0000313|Proteomes:UP000503088};
RN [1] {ECO:0000313|EMBL:QKG85778.1, ECO:0000313|Proteomes:UP000503088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9323 {ECO:0000313|EMBL:QKG85778.1,
RC ECO:0000313|Proteomes:UP000503088};
RA Gulvik C.A., Batra D.G.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of putrescine from agmatine.
CC {ECO:0000256|ARBA:ARBA00054406}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=agmatine + H2O = urea + putrescine; Xref=Rhea:RHEA:13929,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145,
CC ChEBI:CHEBI:326268; EC=3.5.3.11;
CC Evidence={ECO:0000256|ARBA:ARBA00050304};
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 -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC agmatine pathway; putrescine from agmatine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00060523}.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; CP048104; QKG85778.1; -; Genomic_DNA.
DR RefSeq; WP_173224840.1; NZ_CP048104.1.
DR AlphaFoldDB; A0A7D4CQ35; -.
DR KEGG; kpul:GXN76_15830; -.
DR Proteomes; UP000503088; 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 GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd11593; Agmatinase-like_2; 1.
DR FunFam; 3.40.800.10:FF:000004; Agmatinase; 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 Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW Putrescine biosynthesis {ECO:0000256|ARBA:ARBA00023023};
KW Reference proteome {ECO:0000313|Proteomes:UP000503088};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT BINDING 112
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 135
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 139
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 216
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
SQ SEQUENCE 290 AA; 32348 MW; D7166D87016A6D19 CRC64;
MRFDEAYSGN VFIGATPHVE EADIIIYGMP MDWTASFRPG SRFGPKRIRE ASLVLEEYSP
YLDRDLSELN YFDAGDIPLP FGNPEKSLHQ IEAFVDKVLQ QNKIPFGLGG EHLVTWPVVK
AIHRYYSQLA VIHIDAHADL RTDYEGEVLS HATPLRKIVE LLGADNVYQF GIRSGTREEF
HYAKQEKIPF YPFEVLTPLQ RILPQLAGRP VYVTVDIDVL DPAFAPGTGT PEPGGITSRE
LLQAIHSIAD AGIQVVGADL VEVAPVYDPT EQTPVMGAKV LREMLLGFCR
//
