ARCA_PEDPA
ID ARCA_PEDPA Reviewed; 407 AA.
AC Q03DS2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Arginine deiminase {ECO:0000255|HAMAP-Rule:MF_00242};
DE Short=ADI {ECO:0000255|HAMAP-Rule:MF_00242};
DE EC=3.5.3.6 {ECO:0000255|HAMAP-Rule:MF_00242};
DE AltName: Full=Arginine dihydrolase {ECO:0000255|HAMAP-Rule:MF_00242};
DE Short=AD {ECO:0000255|HAMAP-Rule:MF_00242};
GN Name=arcA {ECO:0000255|HAMAP-Rule:MF_00242}; OrderedLocusNames=PEPE_1629;
OS Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS 183-1w).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=278197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine = L-citrulline + NH4(+);
CC Xref=Rhea:RHEA:19597, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:57743; EC=3.5.3.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00242};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_00242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00242}.
CC -!- SIMILARITY: Belongs to the arginine deiminase family.
CC {ECO:0000255|HAMAP-Rule:MF_00242}.
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DR EMBL; CP000422; ABJ68650.1; -; Genomic_DNA.
DR RefSeq; WP_011673771.1; NC_008525.1.
DR AlphaFoldDB; Q03DS2; -.
DR SMR; Q03DS2; -.
DR STRING; 278197.PEPE_1629; -.
DR EnsemblBacteria; ABJ68650; ABJ68650; PEPE_1629.
DR GeneID; 33062580; -.
DR KEGG; ppe:PEPE_1629; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_1_9; -.
DR OMA; ERATMHL; -.
DR OrthoDB; 592329at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000000773; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016990; F:arginine deiminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0018101; P:protein citrullination; IEA:GOC.
DR HAMAP; MF_00242; Arg_deiminase; 1.
DR InterPro; IPR003876; Arg_deiminase.
DR PIRSF; PIRSF006356; Arg_deiminase; 1.
DR PRINTS; PR01466; ARGDEIMINASE.
DR TIGRFAMs; TIGR01078; arcA; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..407
FT /note="Arginine deiminase"
FT /id="PRO_0000336671"
FT ACT_SITE 397
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 407 AA; 45910 MW; D8532ED34A375762 CRC64;
MANAIHVTSE IGKLKTVMLH RPGKEIENIT PDSMERLLFD DIPYLPIAQK EHDFFAKTLT
DQGIEVIYFE KLAADALSDD GVRKEFLNRM IAESGYAVGV IHDALMEYLY AMDPQMMINQ
IIEGVRASDV NIVTPDLQSV SENTDWPFLM DPMPNAYFTR DPQASIGDGL SINKMTFEAR
MRESLITEYI MNYNPRFAGK VKVWRDRNHR THIEGGDELV LNDHVLAIGI SQRTTANAIE
DIARNLFKDS NYDTIIAISI PHNHAMMHLD TVFTMINYEQ FTVHPAILTG DGKVDNWVLH
PGKDGEITME HHTDIKEVLK KALNKSEIDL IPTGNGDPIV APREQWNDGS NTLSIAPGVV
VTYDRNYVSN DLLRQHGILV HEVRSSELSR GRGGPRCMSC PIVREDI