ARGE_LEPBI
ID ARGE_LEPBI Reviewed; 277 AA.
AC P13440;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Putative acetylornithine deacetylase;
DE Short=Acetylornithinase;
DE EC=3.5.1.16;
GN Name=argE;
OS Leptospira biflexa.
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=172;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Patoc I / Serovar Patoc;
RX PubMed=2844724; DOI=10.1128/jb.170.10.4548-4554.1988;
RA Zuerner R.L., Charon N.W.;
RT "Nucleotide sequence analysis of a gene cloned from Leptospira biflexa
RT serovar patoc which complements an argE defect in Escherichia coli.";
RL J. Bacteriol. 170:4548-4554(1988).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine;
CC Xref=Rhea:RHEA:15941, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=3.5.1.16;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC from N(2)-acetyl-L-ornithine (linear): step 1/1.
CC -!- CAUTION: Resembles portions of the beta' subunits of RNA polymerases
CC from bacteria and chloroplasts. It was suggested that both the beta'
CC subunit of RNA polymerases and L.biflexa ArgE-complementing activity
CC possess N-acetylase or N-acetylornithinase activity. No homology with
CC E.coli ArgE. {ECO:0000305}.
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DR EMBL; M22622; AAA25260.1; -; Genomic_DNA.
DR PIR; A31840; A31840.
DR AlphaFoldDB; P13440; -.
DR SMR; P13440; -.
DR UniPathway; UPA00068; UER00110.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR PANTHER; PTHR19376; PTHR19376; 2.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis; Arginine biosynthesis; Hydrolase.
FT CHAIN 1..277
FT /note="Putative acetylornithine deacetylase"
FT /id="PRO_0000064672"
SQ SEQUENCE 277 AA; 31107 MW; 40434BCFA4D7ED63 CRC64;
MNFSKLVVRK MPAHLQKLTV KSKTKVKSLK KNEYYTIIPE TAEQEKVKVA IPIGKQIRVR
QGDFVKRGDQ LDEGNFDPHD ILAIKGPNAL HEYLVSEVQE VYRLQGVHIN DKHIEVVVRS
MLRKVIITDS GDTSFVNQQQ VDKFLFDEEN DRVEKEGGSP AQGTPVLLGL TKASLNTESY
FSAASFQETT KVLTDAAIKG KTDNLMGLKE NVIIGHMIPA GTGMKKYRDI EVFKDLPGDL
DWDLAIGGRG RRSFRTFRVG SCFHCHTLST CCRRGRG