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Database: UniProt
Entry: A0A8B2P0R6_9HYPH
LinkDB: A0A8B2P0R6_9HYPH
Original site: A0A8B2P0R6_9HYPH 
ID   A0A8B2P0R6_9HYPH        Unreviewed;       304 AA.
AC   A0A8B2P0R6;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   08-OCT-2025, entry version 15.
DE   RecName: Full=Arginase {ECO:0000256|ARBA:ARBA00018123, ECO:0000256|NCBIfam:TIGR01229};
DE            EC=3.5.3.1 {ECO:0000256|ARBA:ARBA00012168, ECO:0000256|NCBIfam:TIGR01229};
GN   Name=rocF {ECO:0000313|EMBL:RAI04580.1};
GN   ORFNames=DLJ53_08175 {ECO:0000313|EMBL:RAI04580.1};
OS   Acuticoccus sediminis.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Amorphaceae; Acuticoccus.
OX   NCBI_TaxID=2184697 {ECO:0000313|EMBL:RAI04580.1, ECO:0000313|Proteomes:UP000249590};
RN   [1] {ECO:0000313|EMBL:RAI04580.1, ECO:0000313|Proteomes:UP000249590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PTG4-2 {ECO:0000313|EMBL:RAI04580.1,
RC   ECO:0000313|Proteomes:UP000249590};
RA   Liu X., Lai Q., Du Y., Sun F., Zhang X., Wang S., Shao Z.;
RT   "Acuticoccus sediminis sp. nov., isolated from deep-sea sediment of Indian
RT   Ocean.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine + H2O = urea + L-ornithine; 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:ARBA00047391,
CC         ECO:0000256|RuleBase:RU361159};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036979-1,
CC         ECO:0000256|RuleBase:RU361159};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR036979-1, 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:RU003684}.
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:RAI04580.1}.
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DR   EMBL; QHHQ01000001; RAI04580.1; -; Genomic_DNA.
DR   RefSeq; WP_111343863.1; NZ_QHHQ01000001.1.
DR   AlphaFoldDB; A0A8B2P0R6; -.
DR   OrthoDB; 9788689at2; -.
DR   UniPathway; UPA00158; UER00270.
DR   Proteomes; UP000249590; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004053; F:arginase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:TreeGrafter.
DR   GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd09989; Arginase; 1.
DR   FunFam; 3.40.800.10:FF:000012; 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   InterPro; IPR020855; Ureohydrolase_Mn_BS.
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; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism {ECO:0000256|ARBA:ARBA00022503,
KW   ECO:0000256|RuleBase:RU361159};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR036979-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036979-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249590}.
FT   BINDING         98
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         121
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         123
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         125
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         224
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         226
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
SQ   SEQUENCE   304 AA;  32155 MW;  1D64A4D2F61CE232 CRC64;
     MATMSVLGAP TETGTYRRGC IMGPAAYRTA GLIESLRDLG HVIAEDRDLV PDTVEIDDAA
     HAPAHGVGAT AGWVRAVRRA FAQALARGNV PVLLGGDHSI AAGSLAALMD VAPGTHIVWL
     DAHPDFNTIE TTMSGNLHGI PVAIASGLPG ADLIYGGPIT PLDPRQITMI GIRSVDPDER
     KLLKSHGVTV HDMRDVDEFG MGELIRRAIR RAVEAGARLH VSLDVDFLDP DVAPAVGTTV
     PGGATVREAH LAMELLHESG LVASLDLVEL NPFLDERGRT ATLMVDLAAS LFGRTVMDRP
     TTTW
//
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