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Database: UniProt
Entry: H6RL76_BLASD
LinkDB: H6RL76_BLASD
Original site: H6RL76_BLASD 
ID   H6RL76_BLASD            Unreviewed;       411 AA.
AC   H6RL76;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Arginine deiminase {ECO:0000256|HAMAP-Rule:MF_00242};
DE            Short=ADI {ECO:0000256|HAMAP-Rule:MF_00242};
DE            EC=3.5.3.6 {ECO:0000256|HAMAP-Rule:MF_00242};
DE   AltName: Full=Arginine dihydrolase {ECO:0000256|HAMAP-Rule:MF_00242};
DE            Short=AD {ECO:0000256|HAMAP-Rule:MF_00242};
GN   Name=arcA {ECO:0000256|HAMAP-Rule:MF_00242,
GN   ECO:0000313|EMBL:CCG01206.1};
GN   OrderedLocusNames=BLASA_0227 {ECO:0000313|EMBL:CCG01206.1};
OS   Blastococcus saxobsidens (strain DD2).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG01206.1, ECO:0000313|Proteomes:UP000007517};
RN   [1] {ECO:0000313|EMBL:CCG01206.1, ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|EMBL:CCG01206.1,
RC   ECO:0000313|Proteomes:UP000007517};
RX   PubMed=22535935; DOI=10.1128/JB.00320-12;
RA   Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA   Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA   Gury J., Pujic P., Normand P.;
RT   "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT   Bacterium.";
RL   J. Bacteriol. 194:2752-2753(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA   Genoscope.;
RT   "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00242}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00242}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family.
CC       {ECO:0000256|ARBA:ARBA00010206, ECO:0000256|HAMAP-Rule:MF_00242}.
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DR   EMBL; FO117623; CCG01206.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6RL76; -.
DR   STRING; 1146883.BLASA_0227; -.
DR   KEGG; bsd:BLASA_0227; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_11; -.
DR   OrthoDB; 9807502at2; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000007517; 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   Gene3D; 1.10.3930.10; Arginine deiminase; 1.
DR   HAMAP; MF_00242; Arg_deiminase; 1.
DR   InterPro; IPR003876; Arg_deiminase.
DR   PANTHER; PTHR47271; ARGININE DEIMINASE; 1.
DR   PANTHER; PTHR47271:SF2; ARGININE DEIMINASE; 1.
DR   Pfam; PF02274; ADI; 1.
DR   PIRSF; PIRSF006356; Arg_deiminase; 1.
DR   PRINTS; PR01466; ARGDEIMINASE.
DR   SUPFAM; SSF55909; Pentein; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism {ECO:0000256|HAMAP-Rule:MF_00242};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00242};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007517}.
FT   ACT_SITE        401
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00242,
FT                   ECO:0000256|PIRSR:PIRSR006356-1"
SQ   SEQUENCE   411 AA;  43535 MW;  BD0F5996B9AAEB2A CRC64;
     MIDSAAPLGA TSEVGPLRTV LLHRPGPELR RLTPRNNDQL LFDGVPWVAR AQEEHDAFAQ
     ALTDRGVEVL HLATLLAEVL AFPAARAELI GAAVDDPRLG ATLQRDATRH LAGLAPEDLA
     SALIAGVAHE ELRGHGLAYQ LMDRSDFVVP PLPNLLFTRD SSVWIGDEVA VTSLAMPARH
     RESTITAAIY THHPRFAGAE QLYASSLEHL EGGDVLLLAP GVVAVGVGER TTPGGAERLA
     RRLFARGLAH TVLVVPIAQE RATMHLDTIA TMVDVDAMVM YPAVADSLVA WTVRATDGSP
     THPADDTDTT DLAVTGPQPF LTAAAAAMGI DQLRVIDTGL DPVTAEREQW DDGNNTLALA
     PRLTVAYERN TVTNAALEAA GIEVVRIAGS ELGSGRGGPR CMSCPVSRAP L
//
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