ARCA_HALS3
ID ARCA_HALS3 Reviewed; 486 AA.
AC B0R9X5; Q48294; Q7LY13;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Arginine deiminase;
DE Short=ADI;
DE EC=3.5.3.6;
DE AltName: Full=Arginine dihydrolase;
DE Short=AD;
GN Name=arcA; OrderedLocusNames=OE_5208R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OG Plasmid PHS3.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 376-385; 393-404 AND
RP 442-460, FUNCTION, PATHWAY, AND INDUCTION.
RC STRAIN=R1 / S9 / L33;
RX PubMed=8759859; DOI=10.1128/jb.178.16.4942-4947.1996;
RA Ruepp A., Soppa J.;
RT "Fermentative arginine degradation in Halobacterium salinarium (formerly
RT Halobacterium halobium): genes, gene products, and transcripts of the
RT arcRACB gene cluster.";
RL J. Bacteriol. 178:4942-4947(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1; PLASMID=PHS3;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
CC -!- FUNCTION: Involved in the arginine deiminase pathway of fermentative
CC arginine utilization. {ECO:0000269|PubMed:8759859}.
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 -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC {ECO:0000269|PubMed:8759859}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: No induction in fermentatively grown cells.
CC {ECO:0000269|PubMed:8759859}.
CC -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
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DR EMBL; X80931; CAA56904.1; -; Genomic_DNA.
DR EMBL; AM774418; CAP15556.1; -; Genomic_DNA.
DR PIR; T44863; T44863.
DR RefSeq; WP_010904161.1; NC_010368.1.
DR AlphaFoldDB; B0R9X5; -.
DR SMR; B0R9X5; -.
DR EnsemblBacteria; CAP15556; CAP15556; OE_5208R.
DR GeneID; 5954932; -.
DR GeneID; 62888216; -.
DR KEGG; hsl:OE_5208R; -.
DR HOGENOM; CLU_049514_0_0_2; -.
DR OMA; MHLDTYF; -.
DR PhylomeDB; B0R9X5; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000001321; Plasmid PHS3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016990; F:arginine deiminase activity; IEA:UniProtKB-EC.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0018101; P:protein citrullination; IEA:GOC.
PE 1: Evidence at protein level;
KW Arginine metabolism; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Plasmid.
FT CHAIN 1..486
FT /note="Arginine deiminase"
FT /id="PRO_0000428925"
FT ACT_SITE 476
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 486 AA; 54706 MW; FE6E726E1B60F8A1 CRC64;
MSSESPESVD DSTKVQATAE WDPLQAVRMH LPGAETFVGI MDPEPNLFLN DFSLVDAQQE
HLSLSQDLEA ALPASNPIHY LHDDLANGNG MNALLSSRVN FDLSELGEDE QVNRRDKMWA
RLHELSPHTQ IQAVLGNAEV IRHHSHSDEE VPGSNPDRWD TTSVQLEQPL TNMYFQRDQQ
FVTQNGVVLC SMKEDTRKPE VDIARASWEA LDGDEFDVDI VADMSQVREH DVTEHVPERD
DIQETEVLVE GGDFYPAGEF SLLGVSAKIP EGEAYPKHDI AEDDTEYVHR TTYAAGHRLL
MDDAFGSEEV GLVRAPFEAA QAHKDDDNGE VEMDIMHLDT WFNFVDDDLV VAHKELVENT
TLDVYARTHG GEKPYTLERP DVNFGEYLRE KGFEIVDVYD YVDPSHPDTD MALKAITNFL
TVGPRKILPV RFSDDDDGVM KQFIDGIQED YDVTVIPDGE GRKIINLRAG YGAIHCMTTP
LRRTPE