ARCA_VIBC3
ID ARCA_VIBC3 Reviewed; 407 AA.
AC A5F8P7; C3M4L5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=VC0395_A2842, VC395_0467;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(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; CP000627; ABQ21855.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP08487.1; -; Genomic_DNA.
DR RefSeq; WP_001081182.1; NZ_JAACZH010000015.1.
DR AlphaFoldDB; A5F8P7; -.
DR SMR; A5F8P7; -.
DR STRING; 345073.VC395_0467; -.
DR EnsemblBacteria; ABQ21855; ABQ21855; VC0395_A2842.
DR GeneID; 57739162; -.
DR KEGG; vco:VC0395_A2842; -.
DR KEGG; vcr:VC395_0467; -.
DR PATRIC; fig|345073.21.peg.455; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_0_6; -.
DR OMA; WPARHDE; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000000249; Chromosome 2.
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..407
FT /note="Arginine deiminase"
FT /id="PRO_1000100750"
FT ACT_SITE 397
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 407 AA; 45904 MW; B07EF67C3CED54EF CRC64;
MNRLYVGSEV GQLRRVLLNR PERALTHLTP SNCHELLFDD VLAVEAAGVE HDAFANTLRT
QDVEVLLLHD LLEETLAIPE ARQWLLNTQI SDFRFGPTFA RELRHALNHL DDHHLTTLLL
GGLAFSELHL ESDSMLPKMR QPLDFVIEPL PNHLFTRDTS CWVYGGVSLN PMMKPARQRE
TNHLRAIYRW HPIFAQHPFI HYFGIDDLHY DNANIEGGDV LVIGKGAVLI GMSERTSPQG
VENLAAALFK HGQASKVIAI NLPKHRSCMH LDTVMTHMDV DTFSVYPEVM RKDLPTWRLT
PKGNNGDMRV EQVPSYLHAI EQALGVDYLK IITTGGNSYE AEREQWNDAN NVLTVKPGVV
IGYERNVYTN EKYDKAGIKV LTIPGNELGR GRGGARCMSC PIERDGI
