SPEB2_SYNY3
ID SPEB2_SYNY3 Reviewed; 390 AA.
AC P73270;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable agmatinase 2;
DE EC=3.5.3.11;
DE AltName: Full=Agmatine ureohydrolase 2;
DE Short=AUH 2;
GN Name=speB2; OrderedLocusNames=sll1077;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION.
RX PubMed=10648527; DOI=10.1128/jb.182.4.1008-1015.2000;
RA Quintero M.J., Muro-Pastor A.M., Herrero A., Flores E.;
RT "Arginine catabolism in the cyanobacterium Synechocystis sp. strain PCC
RT 6803 involves the urea cycle and arginase pathway.";
RL J. Bacteriol. 182:1008-1015(2000).
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:0000255|PROSITE-ProRule:PRU00742};
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00742}.
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DR EMBL; BA000022; BAA17298.1; -; Genomic_DNA.
DR PIR; S77451; S77451.
DR PDB; 7ESR; X-ray; 1.42 A; A=1-390.
DR PDB; 7OI1; X-ray; 1.90 A; A/B/C=1-390.
DR PDBsum; 7ESR; -.
DR PDBsum; 7OI1; -.
DR AlphaFoldDB; P73270; -.
DR SMR; P73270; -.
DR IntAct; P73270; 1.
DR STRING; 1148.1652376; -.
DR PaxDb; P73270; -.
DR EnsemblBacteria; BAA17298; BAA17298; BAA17298.
DR KEGG; syn:sll1077; -.
DR eggNOG; COG0010; Bacteria.
DR InParanoid; P73270; -.
DR OMA; CIDAGFV; -.
DR PhylomeDB; P73270; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033389; P:putrescine biosynthetic process from arginine, using agmatinase; IBA:GO_Central.
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 PRINTS; PR00116; ARGINASE.
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; Putrescine biosynthesis;
KW Reference proteome.
FT CHAIN 1..390
FT /note="Probable agmatinase 2"
FT /id="PRO_0000173745"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 291
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 293
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 26..39
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7ESR"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 313..325
FT /evidence="ECO:0007829|PDB:7ESR"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:7ESR"
FT HELIX 346..364
FT /evidence="ECO:0007829|PDB:7ESR"
SQ SEQUENCE 390 AA; 42964 MW; 7612DBDD6C29A133 CRC64;
MSDATPFRPP SEAEEALIKE TRLPLTGWQQ EVDQGLTYGL EAAASIKDRS IPTFSRGELP
HYAGINTFMK APYLEDVREV GKYDVAIVGV PHDSGTTYRP GTRFGPQGIR RISALYTPYN
FEMGVDLREQ ISLCDVGDIF TIPANNEKSF DQISKGIAHI FSSGAFPIIL GGDHSIGFPT
VRGICRHLGD KKVGIIHFDR HVDTQETDLD ERMHTCPWFH ATNMANAPAK NLVQLGIGGW
QVPRQGVKVC RERATNILTV TDITEMSLDA AADFAIARAT DGTDCVWISF DIDCIDAGFV
PGTGWPEPGG LLPREALYLL KRIIRETNVC GMEVVEVSPP YDISDMTSLM ATRVICDTMA
HLVVSGQLPR TEKPAYIHAE ANMAVDEPWQ
