SPEB_ECOLI
ID SPEB_ECOLI Reviewed; 306 AA.
AC P60651; P16936; Q2M9Q6;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Agmatinase;
DE EC=3.5.3.11;
DE AltName: Full=Agmatine ureohydrolase;
DE Short=AUH;
GN Name=speB; OrderedLocusNames=b2937, JW2904;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2153656; DOI=10.1128/jb.172.2.538-547.1990;
RA Szumanski M.B.W., Boyle S.M.;
RT "Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a
RT putrescine biosynthetic enzyme in Escherichia coli.";
RL J. Bacteriol. 172:538-547(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RX PubMed=2198270; DOI=10.1128/jb.172.8.4631-4640.1990;
RA Moore R.C., Boyle S.M.;
RT "Nucleotide sequence and analysis of the speA gene encoding biosynthetic
RT arginine decarboxylase in Escherichia coli.";
RL J. Bacteriol. 172:4631-4640(1990).
RN [5]
RP COFACTOR.
RX PubMed=10329468; DOI=10.1006/bbrc.1999.0709;
RA Carvajal N., Lopez V., Salas M., Uribe E., Herrera P., Cerpa J.;
RT "Manganese is essential for catalytic activity of Escherichia coli
RT agmatinase.";
RL Biochem. Biophys. Res. Commun. 258:808-811(1999).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF HIS-163.
RX PubMed=10527864; DOI=10.1006/bbrc.1999.1505;
RA Carvajal N., Olate J., Salas M., Lopez V., Cerpa J., Herrera P., Uribe E.;
RT "Evidence that histidine-163 is critical for catalytic activity, but not
RT for substrate binding to Escherichia coli agmatinase.";
RL Biochem. Biophys. Res. Commun. 264:196-200(1999).
RN [7]
RP REGULATION.
RX PubMed=1310091; DOI=10.1128/jb.174.3.758-764.1992;
RA Szumanski M.B.W., Boyle S.M.;
RT "Influence of cyclic AMP, agmatine, and a novel protein encoded by a
RT flanking gene on speB (agmatine ureohydrolase) in Escherichia coli.";
RL J. Bacteriol. 174:758-764(1992).
CC -!- FUNCTION: Catalyzes the formation of putrescine from agmatine.
CC {ECO:0000269|PubMed:10527864}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145,
CC ChEBI:CHEBI:326268; EC=3.5.3.11;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10329468};
CC -!- ACTIVITY REGULATION: The expression of auh activity is antagonistically
CC regulated by cyclic AMP and agmatine. In the presence of the cAMP
CC receptor protein, cAMP represses the expression of AUH, while agmatine
CC induces it.
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC agmatine pathway; putrescine from agmatine: step 1/1.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M32363; AAA83909.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69104.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75974.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77000.1; -; Genomic_DNA.
DR EMBL; M31770; AAA24647.1; -; Genomic_DNA.
DR PIR; C42604; C42604.
DR PIR; G85950; G85950.
DR RefSeq; NP_417412.1; NC_000913.3.
DR RefSeq; WP_000105566.1; NZ_STEB01000001.1.
DR PDB; 7LBA; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-306.
DR PDB; 7LOL; X-ray; 1.80 A; A=1-306.
DR PDB; 7LOX; X-ray; 3.20 A; A/B/C=1-306.
DR PDBsum; 7LBA; -.
DR PDBsum; 7LOL; -.
DR PDBsum; 7LOX; -.
DR AlphaFoldDB; P60651; -.
DR SMR; P60651; -.
DR BioGRID; 4260910; 40.
DR DIP; DIP-10906N; -.
DR IntAct; P60651; 7.
DR STRING; 511145.b2937; -.
DR SWISS-2DPAGE; P60651; -.
DR jPOST; P60651; -.
DR PaxDb; P60651; -.
DR PRIDE; P60651; -.
DR EnsemblBacteria; AAC75974; AAC75974; b2937.
DR EnsemblBacteria; BAE77000; BAE77000; BAE77000.
DR GeneID; 67415171; -.
DR GeneID; 947715; -.
DR KEGG; ecj:JW2904; -.
DR KEGG; eco:b2937; -.
DR PATRIC; fig|1411691.4.peg.3796; -.
DR EchoBASE; EB0953; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_039478_0_0_6; -.
DR InParanoid; P60651; -.
DR OMA; YELTTIM; -.
DR PhylomeDB; P60651; -.
DR BioCyc; EcoCyc:AGMATIN-MON; -.
DR BioCyc; MetaCyc:AGMATIN-MON; -.
DR UniPathway; UPA00534; UER00287.
DR PRO; PR:P60651; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008783; F:agmatinase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0033389; P:putrescine biosynthetic process from arginine, using agmatinase; IMP:EcoCyc.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01418; SpeB; 1.
DR InterPro; IPR023694; Agmatinase.
DR InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR11358; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01230; agmatinase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Manganese; Metal-binding; Polyamine biosynthesis;
KW Putrescine biosynthesis; Reference proteome; Spermidine biosynthesis.
FT CHAIN 1..306
FT /note="Agmatinase"
FT /id="PRO_0000173731"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 163
FT /note="Important for catalytic activity"
FT MUTAGEN 163
FT /note="H->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10527864"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:7LBA"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:7LBA"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:7LOL"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:7LBA"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:7LOL"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:7LOL"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:7LOL"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:7LOL"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:7LBA"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:7LOX"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:7LOL"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:7LOL"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:7LBA"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:7LOL"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:7LOL"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:7LOL"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:7LOL"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:7LOL"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:7LOL"
FT HELIX 284..301
FT /evidence="ECO:0007829|PDB:7LOL"
SQ SEQUENCE 306 AA; 33557 MW; 48208BF2CF155570 CRC64;
MSTLGHQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA GGRHGPAAIR
QVSTNLAWEH NRFPWNFDMR ERLNVVDCGD LVYAFGDARE MSEKLQAHAE KLLAAGKRML
SFGGDHFVTL PLLRAHAKHF GKMALVHFDA HTDTYANGCE FDHGTMFYTA PKEGLIDPNH
SVQIGIRTEF DKDNGFTVLD ACQVNDRSVD DVIAQVKQIV GDMPVYLTFD IDCLDPAFAP
GTGTPVIGGL TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ
AAKKGE
