ARCA_OENOB
ID ARCA_OENOB Reviewed; 414 AA.
AC Q04EV5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=OEOE_1118;
OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=203123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-331 / PSU-1;
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; CP000411; ABJ57017.1; -; Genomic_DNA.
DR RefSeq; WP_002823245.1; NC_008528.1.
DR AlphaFoldDB; Q04EV5; -.
DR SMR; Q04EV5; -.
DR STRING; 203123.OEOE_1118; -.
DR EnsemblBacteria; ABJ57017; ABJ57017; OEOE_1118.
DR KEGG; ooe:OEOE_1118; -.
DR PATRIC; fig|203123.7.peg.1140; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_1_9; -.
DR OMA; ERATMHL; -.
DR OrthoDB; 592329at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000000774; 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..414
FT /note="Arginine deiminase"
FT /id="PRO_0000336670"
FT ACT_SITE 402
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 414 AA; 46721 MW; D9656F6EB7F7AAE2 CRC64;
MLTEKSPIHV NSEIGRLKTV ILHRPGKEIE NLTPDTMGPL LFDDIPYLLL AQKEHDNFAD
TLRKKGVEVL YLERLVVQAL ETDEQVKAFF IDKMIAESGF KSGTIHAQLQ KFLVGLPTNE
MVDKIMAGVR FDEIELASKD LQNFSFDRTR PFLMAPMPNL YFTRDPSASI GDGLTINRMT
FKARRRESMF TELVINHHPR FANKNINVWR DRNHVARLEG GDELVLSDHV LAIGLSQRTS
SEAIKDVAKN LFAGSNYDTV IAIQIPQTHA TMHLDTVFTM VNFDQFTVHP MILNNKGELP
ILVMHKDKQN QIKIESSNNL KTVLKEQLGL NELDLISTGD GDPIISAREQ WNDGSNTLAI
APGSVVTYDR NYVSNEALRK HGIQVSEVPS SEISRGRGGP RCMSMPIYRE DIEK