ARCA_PSEAE
ID ARCA_PSEAE Reviewed; 418 AA.
AC P13981;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
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=PA5171;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=2537202; DOI=10.1111/j.1432-1033.1989.tb14520.x;
RA Baur H., Luethi E., Stalon V., Mercenier A., Haas D.;
RT "Sequence analysis and expression of the arginine-deiminase and carbamate-
RT kinase genes of Pseudomonas aeruginosa.";
RL Eur. J. Biochem. 179:53-60(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=2158926; DOI=10.1016/0378-1119(90)90493-b;
RA Luethi E., Baur H., Gamper M., Brunner F., Villeval D., Mercenier A.,
RA Haas D.;
RT "The arc operon for anaerobic arginine catabolism in Pseudomonas aeruginosa
RT contains an additional gene, arcD, encoding a membrane protein.";
RL Gene 87:37-43(1990).
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 -!- ACTIVITY REGULATION: Activated by Mg(2+) or Mn(2+) and strongly
CC inhibited by Zn(2+).
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC -!- SUBUNIT: Homotetramer (Possible).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
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DR EMBL; X14694; CAA32824.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08556.1; -; Genomic_DNA.
DR EMBL; M33223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S02138; S02138.
DR RefSeq; NP_253858.1; NC_002516.2.
DR RefSeq; WP_003111744.1; NZ_QZGE01000002.1.
DR PDB; 1RXX; X-ray; 2.45 A; A/B/C/D=2-418.
DR PDB; 2A9G; X-ray; 2.30 A; A/B/C/D=1-418.
DR PDB; 2AAF; X-ray; 2.30 A; A/B/C/D=1-418.
DR PDB; 2ABR; X-ray; 2.90 A; A/B/C/D=1-418.
DR PDB; 2ACI; X-ray; 2.50 A; A/B/C/D=1-418.
DR PDBsum; 1RXX; -.
DR PDBsum; 2A9G; -.
DR PDBsum; 2AAF; -.
DR PDBsum; 2ABR; -.
DR PDBsum; 2ACI; -.
DR AlphaFoldDB; P13981; -.
DR SMR; P13981; -.
DR STRING; 287.DR97_2539; -.
DR DrugBank; DB04671; [(1S)-4-[[Amino-[(2R)-2-amino-2-carboxyethyl]sulfanylmethylidene]amino]-1-carboxybutyl]azanium.
DR PaxDb; P13981; -.
DR PRIDE; P13981; -.
DR DNASU; 881801; -.
DR EnsemblBacteria; AAG08556; AAG08556; PA5171.
DR GeneID; 881801; -.
DR KEGG; pae:PA5171; -.
DR PATRIC; fig|208964.12.peg.5419; -.
DR PseudoCAP; PA5171; -.
DR HOGENOM; CLU_052662_0_0_6; -.
DR InParanoid; P13981; -.
DR OMA; SAWIYDG; -.
DR PhylomeDB; P13981; -.
DR BioCyc; PAER208964:G1FZ6-5288-MON; -.
DR BRENDA; 3.5.3.6; 5087.
DR SABIO-RK; P13981; -.
DR UniPathway; UPA00254; UER00364.
DR EvolutionaryTrace; P13981; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016990; F:arginine deiminase activity; IMP:PseudoCAP.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019546; P:arginine deiminase pathway; IMP:PseudoCAP.
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 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2537202"
FT CHAIN 2..418
FT /note="Arginine deiminase"
FT /id="PRO_0000182225"
FT ACT_SITE 406
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000250"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1RXX"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:2A9G"
FT TURN 34..41
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:2A9G"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:2A9G"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:2A9G"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:2AAF"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:2A9G"
FT TURN 200..204
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2ABR"
FT STRAND 232..244
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:2A9G"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:2AAF"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:2ABR"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:2A9G"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:2A9G"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:2A9G"
SQ SEQUENCE 418 AA; 46436 MW; D6288249D1B45AB8 CRC64;
MSTEKTKLGV HSEAGKLRKV MVCSPGLAHQ RLTPSNCDEL LFDDVIWVNQ AKRDHFDFVT
KMRERGIDVL EMHNLLTETI QNPEALKWIL DRKITADSVG LGLTSELRSW LESLEPRKLA
EYLIGGVAAD DLPASEGANI LKMYREYLGH SSFLLPPLPN TQFTRDTTCW IYGGVTLNPM
YWPARRQETL LTTAIYKFHP EFANAEFEIW YGDPDKDHGS STLEGGDVMP IGNGVVLIGM
GERSSRQAIG QVAQSLFAKG AAERVIVAGL PKSRAAMHLD TVFSFCDRDL VTVFPEVVKE
IVPFSLRPDP SSPYGMNIRR EEKTFLEVVA ESLGLKKLRV VETGGNSFAA EREQWDDGNN
VVCLEPGVVV GYDRNTYTNT LLRKAGVEVI TISASELGRG RGGGHCMTCP IVRDPIDY
