ARCA_VIBCH
ID ARCA_VIBCH Reviewed; 407 AA.
AC Q9KUU2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=VC_0423;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF93596.1; -; Genomic_DNA.
DR PIR; F82323; F82323.
DR RefSeq; NP_230077.1; NC_002505.1.
DR RefSeq; WP_001081182.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KUU2; -.
DR SMR; Q9KUU2; -.
DR STRING; 243277.VC_0423; -.
DR DNASU; 2615684; -.
DR EnsemblBacteria; AAF93596; AAF93596; VC_0423.
DR GeneID; 57739162; -.
DR KEGG; vch:VC_0423; -.
DR PATRIC; fig|243277.26.peg.398; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_0_6; -.
DR OMA; WPARHDE; -.
DR BioCyc; VCHO:VC0423-MON; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016990; F:arginine deiminase activity; IBA:GO_Central.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019546; P:arginine deiminase pathway; IBA:GO_Central.
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..407
FT /note="Arginine deiminase"
FT /id="PRO_1000100751"
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