ID A0A017RXH9_9CLOT Unreviewed; 408 AA.
AC A0A017RXH9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=Q428_02955 {ECO:0000313|EMBL:EYE89397.1};
OS Fervidicella metallireducens AeB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Fervidicella.
OX NCBI_TaxID=1403537 {ECO:0000313|EMBL:EYE89397.1, ECO:0000313|Proteomes:UP000019681};
RN [1] {ECO:0000313|EMBL:EYE89397.1, ECO:0000313|Proteomes:UP000019681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AeB {ECO:0000313|EMBL:EYE89397.1,
RC ECO:0000313|Proteomes:UP000019681};
RX PubMed=24786951;
RA Patel B.K.;
RT "Draft Genome Sequence of Fervidicella metallireducens Strain AeBT, an
RT Iron-Reducing Thermoanaerobe from the Great Artesian Basin.";
RL Genome Announc. 2:e00345-14(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:EYE89397.1}.
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DR EMBL; AZQP01000005; EYE89397.1; -; Genomic_DNA.
DR RefSeq; WP_035377985.1; NZ_AZQP01000005.1.
DR AlphaFoldDB; A0A017RXH9; -.
DR STRING; 1403537.Q428_02955; -.
DR OrthoDB; 9807502at2; -.
DR UniPathway; UPA00254; UER00364.
DR Proteomes; UP000019681; 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:UP000019681}.
FT ACT_SITE 397
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00242,
FT ECO:0000256|PIRSR:PIRSR006356-1"
SQ SEQUENCE 408 AA; 46403 MW; DEAD6FB46B423038 CRC64;
MDSFINVTSE IGKLKKVMLH RPGREVENLV PEYLGRLLFD DIPYLKIAQQ EHDKFAEVLR
NNGVEVLYLE ELMEESISDE NIKLEFVAEF LEESSITSPA LKEAITQYLL SMSTREMIDS
IISGIRKEEI QLNLRKSLSE LMMDDYPFYL DPMPNLYFTR DPGASIGNGL TLNRMKTEAR
RRETLFLKYI HKYNNRFNKA DVPLWYNRTM PFSLEGGDEL VLSDKVVAIG CSERTSSEAI
EIVAKNLFDG GTSFEKILVF EIPKCRAFMH LDTVFTMVDY DKFTIHPGIQ GPLSVYEITR
GEKGYLNYRH NTSPLEEILK DALKLSSVEL IKCGGGDPII AGREQWNDGS NTLAIAPGVV
VTYERNYVSN ELLEKKGIKV LAIPSSELSR GRGGPRCMSM PLEREVLK
//