ARCA_STRA5
ID ARCA_STRA5 Reviewed; 410 AA.
AC Q8DWQ2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SAG2163;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AE009948; AAN01021.1; -; Genomic_DNA.
DR RefSeq; NP_689148.1; NC_004116.1.
DR RefSeq; WP_000194841.1; NC_004116.1.
DR AlphaFoldDB; Q8DWQ2; -.
DR SMR; Q8DWQ2; -.
DR STRING; 208435.SAG2163; -.
DR EnsemblBacteria; AAN01021; AAN01021; SAG2163.
DR KEGG; sag:SAG2163; -.
DR PATRIC; fig|208435.3.peg.2166; -.
DR HOGENOM; CLU_052662_0_1_9; -.
DR OMA; ERATMHL; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000000821; 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..410
FT /note="Arginine deiminase"
FT /id="PRO_0000182244"
FT ACT_SITE 400
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 410 AA; 46554 MW; 116DEDED8B1DAE8F CRC64;
MTQTHPIHVF SEIGKLKKVM LHRPGKEIEN LMPDYLERLL FDDIPFLEDA QKEHDAFAQA
LRNEGVEVLY LENLAAESLT NQEIREQFID EYIGEANVRG RATKKAIREL LLNIKDNKEL
IEKTMAGIQK SELPEIPSSE KGLTDLVESN YPFAIDPMPN LYFTRDPFAT IGNGVSLNHM
FSETRNRETL YGKYIFTHHP EYGGKVPMVY EREETTRIEG GDELVLSKDV LAVGISQRTD
AASIEKLLVN IFKQNLGFKK VLAFEFANNR KFMHLDTVFT MVDYDKFTIH PEIEGDLRVY
SVTYENQDLH IEEEKGDLAD LLAKNLGVEK VELIRCGGDN LVAAGREQWN DGSNTLTIAP
GVVIVYNRNT ITNAILESKG LKLIKINGSE LVRGRGGPRC MSMPFEREDL