ID I7LFQ3_9CLOT Unreviewed; 405 AA.
AC I7LFQ3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Arginine deiminase {ECO:0000256|HAMAP-Rule:MF_00242};
DE Short=ADI {ECO:0000256|HAMAP-Rule:MF_00242};
DE EC=3.5.3.6 {ECO:0000256|HAMAP-Rule:MF_00242};
DE AltName: Full=Arginine dihydrolase {ECO:0000256|HAMAP-Rule:MF_00242};
DE Short=AD {ECO:0000256|HAMAP-Rule:MF_00242};
GN Name=arcA {ECO:0000256|HAMAP-Rule:MF_00242};
GN ORFNames=CAAU_0601 {ECO:0000313|EMBL:CCJ32685.1};
OS Caloramator australicus RC3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Caloramator.
OX NCBI_TaxID=857293 {ECO:0000313|EMBL:CCJ32685.1, ECO:0000313|Proteomes:UP000007652};
RN [1] {ECO:0000313|EMBL:CCJ32685.1, ECO:0000313|Proteomes:UP000007652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC3 {ECO:0000313|EMBL:CCJ32685.1,
RC ECO:0000313|Proteomes:UP000007652};
RX PubMed=21421756; DOI=10.1128/JB.00193-11;
RA Ogg C.D., Patel B.K.C.;
RT "Draft genome sequence of Caloramator australicus strain RC3T, a
RT thermoanaerobe from the Great Artesian Basin of Australia.";
RL J. Bacteriol. 193:2664-2665(2011).
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:0000256|ARBA:ARBA00001190, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00005213, ECO:0000256|HAMAP-Rule:MF_00242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00242}.
CC -!- SIMILARITY: Belongs to the arginine deiminase family.
CC {ECO:0000256|ARBA:ARBA00010206, ECO:0000256|HAMAP-Rule:MF_00242}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCJ32685.1}.
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DR EMBL; CAKP01000024; CCJ32685.1; -; Genomic_DNA.
DR RefSeq; WP_008907964.1; NZ_CAKP01000024.1.
DR AlphaFoldDB; I7LFQ3; -.
DR STRING; 857293.CAAU_0601; -.
DR eggNOG; COG2235; Bacteria.
DR OrthoDB; 9807502at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000007652; Unassembled WGS sequence.
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 Gene3D; 1.10.3930.10; Arginine deiminase; 1.
DR HAMAP; MF_00242; Arg_deiminase; 1.
DR InterPro; IPR003876; Arg_deiminase.
DR NCBIfam; TIGR01078; arcA; 1.
DR PANTHER; PTHR47271; ARGININE DEIMINASE; 1.
DR PANTHER; PTHR47271:SF2; ARGININE DEIMINASE; 1.
DR Pfam; PF02274; ADI; 1.
DR PIRSF; PIRSF006356; Arg_deiminase; 1.
DR PRINTS; PR01466; ARGDEIMINASE.
DR SUPFAM; SSF55909; Pentein; 1.
PE 3: Inferred from homology;
KW Arginine metabolism {ECO:0000256|ARBA:ARBA00022503, ECO:0000256|HAMAP-
KW Rule:MF_00242}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00242};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007652}.
FT ACT_SITE 395
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00242,
FT ECO:0000256|PIRSR:PIRSR006356-1"
SQ SEQUENCE 405 AA; 45973 MW; 6F91E23DB344D843 CRC64;
MKHFINVTSE IGRLKRVLLH RPGQEVENLV PEYLGRLLFD DIPYLKIAQQ EHDKFAQVLR
ENGAEVVYLE ELSAEVLEDE KVKLEFLKEF LEESGITSPS LKESLIEYLS KMPARQMVDK
IMAGVRKNEI EVKEPTSLVE LMADDYPFYL DPMPNLYFTR DPGASIGNGI TLNRMRTEAR
RRETLFLKYI IKYHKSFEGI PLWYDRSMPY AIEGGDELVL SDKVVAIGCS ERTSAEAIEM
VARNLFNANT SFEKVLVFEI PKCRAFMHLD TVFTMVDYDK FTIHPGVQGP LSVYEVTKGA
NNTIKFKHNT SPLNKILAEA LNLSSVELIQ CGGGDFIIAG REQWNDGSNT LAIAPGVVVT
YERNYVTNEI LTKRGIKVIT IPSSELSRGR GGPRCMSMPL YREKL
//