ID   ARCA_META1              Reviewed;         409 AA.
AC   B3PNI8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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};
GN   OrderedLocusNames=MARTH_orf873;
OS   Metamycoplasma arthritidis (strain 158L3-1) (Mycoplasma arthritidis).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC   Metamycoplasma.
OX   NCBI_TaxID=243272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=158L3-1;
RX   PubMed=18573899; DOI=10.1128/iai.00516-08;
RA   Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H.,
RA   Loraine A.E.;
RT   "Genome of Mycoplasma arthritidis.";
RL   Infect. Immun. 76:4000-4008(2008).
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; CP001047; ACF07590.1; -; Genomic_DNA.
DR   RefSeq; WP_012498547.1; NC_011025.1.
DR   AlphaFoldDB; B3PNI8; -.
DR   SMR; B3PNI8; -.
DR   STRING; 243272.MARTH_orf873; -.
DR   EnsemblBacteria; ACF07590; ACF07590; MARTH_orf873.
DR   KEGG; mat:MARTH_orf873; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_14; -.
DR   OMA; ERATMHL; -.
DR   OrthoDB; 592329at2; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000008812; 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..409
FT                   /note="Arginine deiminase"
FT                   /id="PRO_1000100740"
FT   ACT_SITE        398
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ   SEQUENCE   409 AA;  46068 MW;  8FE5D9D32462A4FD CRC64;
     MSVFDSKFKG IHVYSEIGEL ETVLVHEPGK EIDYITPARL DELLFSAILE SHDARKEHKE
     FVAELKKRGI NVVELVDLIV ETYDLASKEA KEKLLEEFLD DSVPVLSDEH RAAVKKFLQS
     QKSTRSLVEY MIAGITKHDL KIESDLELIV DPMPNLYFTR DPFASVGNGV TIHYMRYKVR
     QRETLFSRFV FSNHPKLVNT PWYYDPAEGL SIEGGDVFIY NNDTLVVGVS ERTDLQTITL
     LAKNIKANKE CEFKRIVAIN VPKWTNLMHL DTWLTMLDKD KFLYSPIAND VFKFWDYDLV
     NGGDAPQPVD NGLPLEDLLK SIIGKKPTLI PIAGAGASQI DIERETHFDG TNYLAVAPGI
     VIGYARNEKT NAALEAAGIT VLPFRGNQLS LGMGNARCMS MPLSRKDVK