ID   ARCA_BURMA              Reviewed;         418 AA.
AC   Q62KD9;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=BMA1145;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000010; AAU47428.1; -; Genomic_DNA.
DR   RefSeq; WP_004526983.1; NC_006348.1.
DR   RefSeq; YP_102830.1; NC_006348.1.
DR   AlphaFoldDB; Q62KD9; -.
DR   SMR; Q62KD9; -.
DR   STRING; 243160.BMA1145; -.
DR   EnsemblBacteria; AAU47428; AAU47428; BMA1145.
DR   GeneID; 56595528; -.
DR   KEGG; bma:BMA1145; -.
DR   PATRIC; fig|243160.12.peg.1177; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_0_4; -.
DR   OMA; SAWIYDG; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000006693; Chromosome 1.
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.
FT   CHAIN           1..418
FT                   /note="Arginine deiminase"
FT                   /id="PRO_0000182206"
FT   ACT_SITE        406
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   418 AA;  46052 MW;  BD093EE12D6B9871 CRC64;
     MSQAIPQVGV HSEVGKLRKV LVCSPGLAHQ RLTPSNCDEL LFDDVMWVNQ AKRDHFDFVS
     KMRERGVEVL EMHNLLTETV QNPAALKWIL DRKITPDNVG IGLVDEVRAW LEGLEPRALA
     EFLIGGVAAS DIAGAERSKV LTLFRDYLGK SSFVLPPLPN MMFTRDTSCW IYGGVTLNPM
     HWPARRQETL LVAAVYKFHP AFTDAKFDVW YGDPDRDHGM ATLEGGDVMP IGRGVVLVGM
     GERTSRQAVG QLAQALFAKG AAERVIVAGL PNSRASMHLD TVFSFCDRDL VTVFPEVVNR
     IVPFTLRPGG DARYGIDIER EDKPFVDVVA QALGLKSLRV VETGGNDFAA EREQWDDGNN
     MVCIEPGVVV GYDRNTYTNT LLRKAGVEVI TIGSSELGRG RGGGHCMTCP VLRDPVDY