ARCA_ALISL
ID ARCA_ALISL Reviewed; 406 AA.
AC B6EMS7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=VSAL_I0521;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(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; FM178379; CAQ78206.1; -; Genomic_DNA.
DR RefSeq; WP_012549330.1; NC_011312.1.
DR AlphaFoldDB; B6EMS7; -.
DR SMR; B6EMS7; -.
DR STRING; 316275.VSAL_I0521; -.
DR EnsemblBacteria; CAQ78206; CAQ78206; VSAL_I0521.
DR KEGG; vsa:VSAL_I0521; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_0_6; -.
DR OMA; ERATMHL; -.
DR OrthoDB; 592329at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000001730; Chromosome 1.
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..406
FT /note="Arginine deiminase"
FT /id="PRO_1000100734"
FT ACT_SITE 396
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 406 AA; 46144 MW; D254B43B0890BF23 CRC64;
MSKLFVGSEI GQLRRVILHR PERALSHLTP TNCHNLLFDD VLSVEKALHE HDQFVATLRQ
QDVEVLLLQD LLEETLAHPE AKQWLLRHQI SHYRFGPTFA NQIRAFLLEK NNKELASILL
GGLAFIELPF KAPSMLQQLS DPFDFVIDPL PNHLFTRDTS CWIYGGVSIN PMAKAARKRE
SNHLRAIYKW HPLFSNQSFP RYFGDENRHY DNATIEGGDV LIIGKGNVLV GISERTTPQG
IENLAKQLFR TEQAKQVIAI KLPENRSCMH LDTVMTHMDH NVFSVYPRVI DKNMPCWSIT
PCGDQQLAIQ EKPNFEHSLM QALELDSLNI ITTGGDSYEA EREQWHDANN VLTIKPGVVV
AYERNVYTNE KYDKAGITVL PIMGDELGRG RGGARCMSCP IERDGI