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Database: UniProt
Entry: A0A2M8T879_9CLOT
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Original site: A0A2M8T879_9CLOT 
ID   A0A2M8T879_9CLOT        Unreviewed;       307 AA.
AC   A0A2M8T879;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Arginase {ECO:0000256|ARBA:ARBA00018123, ECO:0000256|RuleBase:RU361159};
DE            EC=3.5.3.1 {ECO:0000256|ARBA:ARBA00012168, ECO:0000256|RuleBase:RU361159};
GN   Name=rocF {ECO:0000313|EMBL:PJI07197.1};
GN   ORFNames=CUB90_04660 {ECO:0000313|EMBL:PJI07197.1};
OS   Clostridium sp. CT7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=2052574 {ECO:0000313|EMBL:PJI07197.1, ECO:0000313|Proteomes:UP000230839};
RN   [1] {ECO:0000313|EMBL:PJI07197.1, ECO:0000313|Proteomes:UP000230839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT7 {ECO:0000313|EMBL:PJI07197.1,
RC   ECO:0000313|Proteomes:UP000230839};
RA   Xin F., Chen T.;
RT   "The draft genome sequence of Clostridium sp. CT7, a unique bacterium
RT   capable of producing butanol from glycerol uncoupled acetone and 1,3-
RT   propanediol formation.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:46911; EC=3.5.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000227,
CC         ECO:0000256|RuleBase:RU361159};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361159};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000256|RuleBase:RU361159};
CC   -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC       arginine: step 1/1. {ECO:0000256|ARBA:ARBA00005098}.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU361159}.
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:PJI07197.1}.
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DR   EMBL; PETE01000002; PJI07197.1; -; Genomic_DNA.
DR   RefSeq; WP_066020103.1; NZ_PETE01000002.1.
DR   AlphaFoldDB; A0A2M8T879; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000230839; Unassembled WGS sequence.
DR   GO; GO:0004053; F:arginase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd09989; Arginase; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR014033; Arginase.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   NCBIfam; TIGR01229; rocF_arginase; 1.
DR   PANTHER; PTHR43782; ARGINASE; 1.
DR   PANTHER; PTHR43782:SF3; ARGINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
DR   PRINTS; PR00116; ARGINASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism {ECO:0000256|ARBA:ARBA00022503,
KW   ECO:0000256|RuleBase:RU361159}; Hydrolase {ECO:0000256|RuleBase:RU361159};
KW   Manganese {ECO:0000256|RuleBase:RU361159};
KW   Metal-binding {ECO:0000256|RuleBase:RU361159};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230839}.
SQ   SEQUENCE   307 AA;  34021 MW;  1F34356B1D3DFCF1 CRC64;
     MNIDILGVPI YYGSDKKGVD LAPNKIREDN LKAVITKYNH KVRDMGNVSV PFIPEKDKFN
     DNSKMKFLKP IMKVNKDVAD EVYHSLASGD FPFILGGDHS IGLGSISGAS KFDKDLAVIW
     IDAHTDINTD KTTLSGNVHG MPLAAAMGIG SNELTDIYYK GQKVKPENVF IIGARDIDDG
     ESKLISEKHL NVYSTETLKK IGVKNIMDEI HKKLLSQNVH SVHLSLDIDC LDKSIVPGTG
     TPVPNGMSIP DTKFIISYLA KTGLVKSMDL VEFNVLLDKN SETENVVMDF IDWTFKNLKR
     NSNDVEH
//
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