ARCA_MYCAR
ID ARCA_MYCAR Reviewed; 410 AA.
AC P23793;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 118.
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;
OS Mycoplasmopsis arginini (Mycoplasma arginini).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=2094;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 23838 / CIP 71.23 / NBRC 14476 / NCTC 10129 / G230;
RX PubMed=7765234; DOI=10.1016/0168-1656(94)90050-7;
RA Misawa S., Aoshima M., Takaku H., Matsumoto M., Hayashi H.;
RT "High-level expression of Mycoplasma arginine deiminase in Escherichia coli
RT and its efficient renaturation as an anti-tumor enzyme.";
RL J. Biotechnol. 36:145-155(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2228248; DOI=10.1128/iai.58.11.3788-3795.1990;
RA Ohno T., Ando O., Sugimura K., Taniai M., Suzuki M., Fukuda S., Nagase Y.,
RA Yamamoto K., Azuma I.;
RT "Cloning and nucleotide sequence of the gene encoding arginine deiminase of
RT Mycoplasma arginini.";
RL Infect. Immun. 58:3788-3795(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=KM101;
RX PubMed=2325633; DOI=10.1007/bf00280371;
RA Kondo K., Sone H., Yoshida H., Toida T., Kanatani K., Hong Y.-M.,
RA Nishino N., Tanaka J.;
RT "Cloning and sequence analysis of the arginine deiminase gene from
RT Mycoplasma arginini.";
RL Mol. Gen. Genet. 221:81-86(1990).
RN [4]
RP PROTEIN SEQUENCE OF 2-18.
RX PubMed=2164440;
RA Miyazaki K., Takaku H., Umeda M., Fujita T., Huang W.D., Kimura T.,
RA Yamashita J., Horio T.;
RT "Potent growth inhibition of human tumor cells in culture by arginine
RT deiminase purified from a culture medium of a Mycoplasma-infected cell
RT line.";
RL Cancer Res. 50:4522-4527(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 -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the arginine deiminase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X54141; CAA38080.1; -; Genomic_DNA.
DR EMBL; X54312; CAA38210.1; -; Genomic_DNA.
DR EMBL; X52459; CAA36693.2; -; Genomic_DNA.
DR PIR; A41465; A41465.
DR RefSeq; WP_004416214.1; NZ_LR215044.1.
DR PDB; 1LXY; X-ray; 2.00 A; A/B=2-410.
DR PDB; 1S9R; X-ray; 1.60 A; A/B=1-410.
DR PDBsum; 1LXY; -.
DR PDBsum; 1S9R; -.
DR AlphaFoldDB; P23793; -.
DR SMR; P23793; -.
DR STRING; 1188236.MARG_2120; -.
DR eggNOG; COG2235; Bacteria.
DR OrthoDB; 592329at2; -.
DR BRENDA; 3.5.3.6; 3521.
DR SABIO-RK; P23793; -.
DR UniPathway; UPA00254; UER00364.
DR EvolutionaryTrace; P23793; -.
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 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Cytoplasm; Direct protein sequencing;
KW Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2164440"
FT CHAIN 2..410
FT /note="Arginine deiminase"
FT /id="PRO_0000182219"
FT ACT_SITE 398
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000250"
FT CONFLICT 76
FT /note="I -> T (in Ref. 3; CAA36693)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="A -> S (in Ref. 3; CAA36693)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="E -> K (in Ref. 2; CAA38210)"
FT /evidence="ECO:0000305"
FT CONFLICT 375..410
FT /note="EAAGIKVLPFHGNQLSLGMGNARCMSMPLSRKDVKW -> DKKDYLRPISI
FT (in Ref. 3; CAA36693)"
FT /evidence="ECO:0000305"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:1S9R"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:1S9R"
FT TURN 195..199
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 221..232
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1S9R"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:1S9R"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 339..347
FT /evidence="ECO:0007829|PDB:1S9R"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 368..376
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:1S9R"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:1S9R"
FT TURN 396..399
FT /evidence="ECO:0007829|PDB:1S9R"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:1S9R"
SQ SEQUENCE 410 AA; 46507 MW; E15C9A8AC90176FA CRC64;
MSVFDSKFKG IHVYSEIGEL ESVLVHEPGR EIDYITPARL DELLFSAILE SHDARKEHKQ
FVAELKANDI NVVELIDLVA ETYDLASQEA KDKLIEEFLE DSEPVLSEEH KVVVRNFLKA
KKTSRELVEI MMAGITKYDL GIEADHELIV DPMPNLYFTR DPFASVGNGV TIHYMRYKVR
QRETLFSRFV FSNHPKLINT PWYYDPSLKL SIEGGDVFIY NNDTLVVGVS ERTDLQTVTL
LAKNIVANKE CEFKRIVAIN VPKWTNLMHL DTWLTMLDKD KFLYSPIAND VFKFWDYDLV
NGGAEPQPVE NGLPLEGLLQ SIINKKPVLI PIAGEGASQM EIERETHFDG TNYLAIRPGV
VIGYSRNEKT NAALEAAGIK VLPFHGNQLS LGMGNARCMS MPLSRKDVKW
