ARCA_STRPD
ID ARCA_STRPD Reviewed; 411 AA.
AC Q1JFY9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=MGAS10270_Spy1290;
OS Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370552;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10270;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(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; CP000260; ABF34355.1; -; Genomic_DNA.
DR RefSeq; WP_011888729.1; NC_008022.1.
DR AlphaFoldDB; Q1JFY9; -.
DR SMR; Q1JFY9; -.
DR EnsemblBacteria; ABF34355; ABF34355; MGAS10270_Spy1290.
DR KEGG; sph:MGAS10270_Spy1290; -.
DR HOGENOM; CLU_052662_0_1_9; -.
DR OMA; ERATMHL; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000002436; 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.
FT CHAIN 1..411
FT /note="Arginine deiminase"
FT /id="PRO_1000005727"
FT ACT_SITE 401
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 411 AA; 46311 MW; 7011E3E1A03649C0 CRC64;
MTAQTPIHVY SEIGKLKKVL LHRPGKEIEN LMPDYLERLL FDDIPFLEDA QKEHDAFAQA
LRDEGIEVLY LETLAAESLV TPEIREAFID EYLSEANIRG RATKKAIREL LMAIEDNQEL
IEKTMAGVQK SELPEIPASE KGLTDLVESN YPFAIDPMPN LYFTRDPFAT IGTGVSLNHM
FSETRNRETL YGKYIFTHHP IYGGGKVPMV YDRNETTRIE GGDELVLSKD VLAVGISQRT
DAASIEKLLV NIFKQNLGFK KVLAFEFANN RKFMHLDTVF TMVDYDKFTI HPEIEGDLRV
YSVTYDNEEL HIIEEKGDLA ELLAANLGVE KVDLIRCGGD NLVAAGREQW NDGSNTLTIA
PGVVVVYNRN TITNAILESK GLKLIKIHGS ELVRGRGGPR CMSMPFERED I