ARCA_LIMF3
ID ARCA_LIMF3 Reviewed; 407 AA.
AC B2GAF4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Arginine deiminase {ECO:0000255|HAMAP-Rule:MF_00242};
DE Short=ADI {ECO:0000255|HAMAP-Rule:MF_00242};
DE EC=3.5.3.6 {ECO:0000255|HAMAP-Rule:MF_00242};
DE AltName: Full=Arginine dihydrolase {ECO:0000255|HAMAP-Rule:MF_00242};
DE Short=AD {ECO:0000255|HAMAP-Rule:MF_00242};
GN Name=arcA {ECO:0000255|HAMAP-Rule:MF_00242}; OrderedLocusNames=LAF_0300;
OS Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS fermentum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=334390;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3956 / LMG 18251;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(2008).
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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00242}.
CC -!- SIMILARITY: Belongs to the arginine deiminase family.
CC {ECO:0000255|HAMAP-Rule:MF_00242}.
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DR EMBL; AP008937; BAG26636.1; -; Genomic_DNA.
DR RefSeq; WP_004563316.1; NC_010610.1.
DR AlphaFoldDB; B2GAF4; -.
DR SMR; B2GAF4; -.
DR EnsemblBacteria; BAG26636; BAG26636; LAF_0300.
DR GeneID; 61200534; -.
DR KEGG; lfe:LAF_0300; -.
DR eggNOG; COG2235; Bacteria.
DR HOGENOM; CLU_052662_0_1_9; -.
DR OMA; ERATMHL; -.
DR OrthoDB; 592329at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000001697; Chromosome.
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 3: Inferred from homology;
KW Arginine metabolism; Cytoplasm; Hydrolase.
FT CHAIN 1..407
FT /note="Arginine deiminase"
FT /id="PRO_1000100738"
FT ACT_SITE 397
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00242"
SQ SEQUENCE 407 AA; 45949 MW; E1EEBEBA3118006C CRC64;
MTSPIHVTSE IGKLKTVMLH RPGREIENIT PDYMERLLFD DIPYLPIAQE EHDFFAQTLR
DQGIEVLYFE KLAAEALASD DVRKEFLNRM IAESGYVAGT THDALYDYLY QMTPQEMVDK
IIEGVRGTDI DIAQPDLQSV SENTDWPFLM DPMPNAYFTR DPQASIGDGI SINKMTFPAR
QRESLITEYI INHHPRFAGQ VEVWRDRNHE SHIEGGDELV LSDHVLAIGV SQRTTADAIE
DIARNLFKDS NYDTVIAISI PHNHAMMHLD TVFTMINHDQ FTVHPAILDD KGEVDNWVLH
PGKDGEITIE HHTDIKAVLK QALNKPEIDL IPTGNGDPIV APREQWNDGS NTLAIAPGEV
VTYNRNYVSN ALLKEHGILV HEVRSSELSR GRGGPRCMSC PIVREDL