ARCA_STRPY
ID ARCA_STRPY Reviewed; 411 AA.
AC P0C0B3; P16962; P68769;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Arginine deiminase;
DE Short=ADI;
DE EC=3.5.3.6;
DE AltName: Full=Arginine dihydrolase;
DE Short=AD;
DE AltName: Full=Streptococcal acid glycoprotein;
GN Name=arcA; Synonyms=sagP;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26.
RC STRAIN=ATCC 21060 / Su / DSM 2072;
RA Kanaoka M., Kawanaka C., Negoro T., Fukita Y., Taya K., Agui H.;
RT "Cloning and expression of the antitumor glycoprotein gene of Streptococcus
RT pyogenes Su in Escherichia coli.";
RL Agric. Biol. Chem. 51:2641-2648(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, AND SUBUNIT.
RX PubMed=1368629; DOI=10.1271/bbb1961.55.743;
RA Kanaoka M., Negoro T., Kawanaka C., Agui H., Nabeshima S.;
RT "Streptococcal antitumor protein: expression in Escherichia coli cells and
RT properties of the recombinant protein.";
RL Agric. Biol. Chem. 55:743-750(1991).
CC -!- FUNCTION: Antitumor protein. Has a powerful and dose-dependent
CC inhibitory effect on antigen, superantigen, or mitogen-stimulated human
CC peripheral blood mononuclear cell (PBMC) proliferation. It may inhibit
CC cell proliferation by arresting cell cycle and inducing apoptosis (By
CC similarity). {ECO:0000250}.
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 -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC -!- SUBUNIT: Homotetramer. The recombinant protein is a homodimer.
CC {ECO:0000269|PubMed:1368629}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
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DR EMBL; D13790; BAA02938.1; -; Genomic_DNA.
DR EMBL; X55659; CAA39192.1; -; Genomic_DNA.
DR PIR; A38835; A38835.
DR RefSeq; WP_002983803.1; NZ_WXZI01000007.1.
DR PDB; 4BOF; X-ray; 2.48 A; A/B/C/D/E/F/G/H=1-411.
DR PDBsum; 4BOF; -.
DR AlphaFoldDB; P0C0B3; -.
DR SMR; P0C0B3; -.
DR GeneID; 57852966; -.
DR GeneID; 66901284; -.
DR eggNOG; COG2235; Bacteria.
DR OMA; ERATMHL; -.
DR UniPathway; UPA00254; UER00364.
DR PHI-base; PHI:8635; -.
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 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Cytoplasm; Direct protein sequencing;
KW Glycoprotein; Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..411
FT /note="Arginine deiminase"
FT /id="PRO_0000182247"
FT ACT_SITE 401
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000250"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:4BOF"
FT TURN 26..30
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4BOF"
FT TURN 36..40
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:4BOF"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:4BOF"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:4BOF"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 342..350
FT /evidence="ECO:0007829|PDB:4BOF"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 371..379
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:4BOF"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:4BOF"
FT TURN 399..402
FT /evidence="ECO:0007829|PDB:4BOF"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:4BOF"
SQ SEQUENCE 411 AA; 46297 MW; 9182F04A238E7243 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 HIVEEKGDLA ELLAANLGVE KVDLIRCGGD NLVAAGREQW NDGSNTLTIA
PGVVVVYNRN TITNAILESK GLKLIKIHGS ELVRGRGGPR CMSMPFERED I
