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Database: UniProt
Entry: A0A0C1TXU5_9CLOT
LinkDB: A0A0C1TXU5_9CLOT
Original site: A0A0C1TXU5_9CLOT 
ID   A0A0C1TXU5_9CLOT        Unreviewed;       403 AA.
AC   A0A0C1TXU5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   ECO:0000313|EMBL:KIE45514.1};
GN   ORFNames=U732_2502 {ECO:0000313|EMBL:KIE45514.1};
OS   Clostridium argentinense CDC 2741.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE45514.1, ECO:0000313|Proteomes:UP000031366};
RN   [1] {ECO:0000313|EMBL:KIE45514.1, ECO:0000313|Proteomes:UP000031366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE45514.1,
RC   ECO:0000313|Proteomes:UP000031366};
RX   PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA   Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA   Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA   Karavis M.A., Smith L.A.;
RT   "Genomic sequences of six botulinum neurotoxin-producing strains
RT   representing three clostridial species illustrate the mobility and
RT   diversity of botulinum neurotoxin genes.";
RL   Infect. Genet. Evol. 30:102-113(2014).
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:KIE45514.1}.
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DR   EMBL; AYSO01000019; KIE45514.1; -; Genomic_DNA.
DR   RefSeq; WP_039634991.1; NZ_AYSO01000019.1.
DR   AlphaFoldDB; A0A0C1TXU5; -.
DR   STRING; 29341.RSJ17_00720; -.
DR   OrthoDB; 9807502at2; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000031366; 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:UP000031366}.
FT   ACT_SITE        391
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00242,
FT                   ECO:0000256|PIRSR:PIRSR006356-1"
SQ   SEQUENCE   403 AA;  46690 MW;  24EA10C5516E2C37 CRC64;
     MEKRNIEVYS EIGNLKTVLL HRPGKEIENL TPEYLERLLF DDIPYLKIAR DEHDKFADLF
     KINGVEVLYL ENLVAEVVKN SEIKKRFINE IICESNIEKD YIKNEIKSYL LSMLPKEMID
     TVMAGVRKID ISMKESSNEY PFLLDPMPNL YFTRDPFACI GNGVSLNSMK KPIRRRESIF
     GKYIFKYHPH FKDSNIKIYY DREDEFHIEG GDQLVLSKDV LAVGYSERTD KEAIFTLAKN
     VFKANESFKN ILIFDIPKIR AFMHLDTVFT MVDYDKFTIH PAIEASLKVT NLSYDKTKNE
     IVAMEEEDSL EAILSKYLGR DITLIRCGNG DQIISGREQW NDGSNTLAIS PGKVITYDRN
     YVTNELLDKH NIEVFSIASS ELSRGRGGPR CMSMPFIREE LKY
//
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