PAH_STRCL
ID PAH_STRCL Reviewed; 313 AA.
AC P0DJQ3; P0DJQ4; P37819; P72400;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Proclavaminate amidinohydrolase;
DE EC=3.5.3.22 {ECO:0000269|PubMed:12020346};
DE AltName: Full=Proclavaminic acid amidino hydrolase;
GN Name=pah;
OS Streptomyces clavuligerus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1901;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8529893; DOI=10.1016/0378-1119(95)00560-9;
RA Hodgson J.E., Fosberry A.P., Rawlinson N.S., Ross H.N.M., Neal R.J.,
RA Arnell J.C., Earl A.J., Lawlor E.J.;
RT "Clavulanic acid biosynthesis in Streptomyces clavuligerus: gene cloning
RT and characterization.";
RL Gene 166:49-55(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC 3585 / VKM Ac-602;
RX PubMed=8088547; DOI=10.1016/0378-1119(94)90036-1;
RA Aidoo K.A., Wong A., Alexander D.C., Rittammer R.A.R., Jensen S.E.;
RT "Cloning, sequencing and disruption of a gene from Streptomyces
RT clavuligerus involved in clavulanic acid biosynthesis.";
RL Gene 147:41-46(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MANGANESE, PROTEIN
RP SEQUENCE OF 1-6, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=12020346; DOI=10.1042/bj20020125;
RA Elkins J.M., Clifton I.J., Hernandez H., Doan L.X., Robinson C.V.,
RA Schofield C.J., Hewitson K.S.;
RT "Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of
RT a hydrolytic enzyme in clavulanic acid biosynthesis.";
RL Biochem. J. 366:423-434(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=amidinoproclavaminate + H2O = proclavaminate + urea;
CC Xref=Rhea:RHEA:17001, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:57302, ChEBI:CHEBI:58647; EC=3.5.3.22;
CC Evidence={ECO:0000269|PubMed:12020346};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742,
CC ECO:0000269|PubMed:12020346};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742, ECO:0000269|PubMed:12020346};
CC -!- PATHWAY: Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate
CC from D-glyceraldehyde 3-phosphate and L-arginine: step 4/8.
CC {ECO:0000305|PubMed:12020346}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:12020346}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; X84101; CAA58904.1; -; Genomic_DNA.
DR EMBL; U87786; AAA62451.1; -; Genomic_DNA.
DR PIR; S57669; S57669.
DR RefSeq; WP_003952511.1; NZ_CP032052.1.
DR PDB; 1GQ6; X-ray; 1.75 A; A/B/C=1-313.
DR PDB; 1GQ7; X-ray; 2.45 A; A/B/C/D/E/F=1-313.
DR PDBsum; 1GQ6; -.
DR PDBsum; 1GQ7; -.
DR AlphaFoldDB; P0DJQ3; -.
DR SMR; P0DJQ3; -.
DR STRING; 443255.SCLAV_4195; -.
DR GeneID; 61469725; -.
DR eggNOG; COG0010; Bacteria.
DR OMA; PITPFDA; -.
DR OrthoDB; 1598732at2; -.
DR BioCyc; MetaCyc:MON-13488; -.
DR BRENDA; 3.5.3.22; 5988.
DR UniPathway; UPA00112; UER00245.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033972; F:proclavaminate amidinohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0033050; P:clavulanic acid biosynthetic process; IEA:UniProtKB-UniPathway.
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 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; Direct protein sequencing; Hydrolase; Manganese;
KW Metal-binding.
FT CHAIN 1..313
FT /note="Proclavaminate amidinohydrolase"
FT /id="PRO_0000173746"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12020346,
FT ECO:0007744|PDB:1GQ6, ECO:0007744|PDB:1GQ7"
FT BINDING 144
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12020346,
FT ECO:0007744|PDB:1GQ6, ECO:0007744|PDB:1GQ7"
FT BINDING 144
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12020346,
FT ECO:0007744|PDB:1GQ6, ECO:0007744|PDB:1GQ7"
FT BINDING 146
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12020346,
FT ECO:0007744|PDB:1GQ6, ECO:0007744|PDB:1GQ7"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12020346,
FT ECO:0007744|PDB:1GQ6, ECO:0007744|PDB:1GQ7"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12020346,
FT ECO:0007744|PDB:1GQ6, ECO:0007744|PDB:1GQ7"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12020346,
FT ECO:0007744|PDB:1GQ6, ECO:0007744|PDB:1GQ7"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12020346,
FT ECO:0007744|PDB:1GQ6, ECO:0007744|PDB:1GQ7"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1GQ7"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1GQ7"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 93..110
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 172..183
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1GQ6"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:1GQ7"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 206..225
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:1GQ6"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:1GQ6"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1GQ6"
FT HELIX 289..308
FT /evidence="ECO:0007829|PDB:1GQ6"
SQ SEQUENCE 313 AA; 33401 MW; 759E9B5644B88D5E CRC64;
MERIDSHVSP RYAQIPTFMR LPHDPQPRGY DVVVIGAPYD GGTSYRPGAR FGPQAIRSES
GLIHGVGIDR GPGTFDLINC VDAGDINLTP FDMNIAIDTA QSHLSGLLKA NAAFLMIGGD
HSLTVAALRA VAEQHGPLAV VHLDAHSDTN PAFYGGRYHH GTPFRHGIDE KLIDPAAMVQ
IGIRGHNPKP DSLDYARGHG VRVVTADEFG ELGVGGTADL IREKVGQRPV YVSVDIDVVD
PAFAPGTGTP APGGLLSREV LALLRCVGDL KPVGFDVMEV SPLYDHGGIT SILATEIGAE
LLYQYARAHR TQL
