ID Q6ANF4_DESPS Unreviewed; 344 AA.
AC Q6ANF4;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Related to agmatinase {ECO:0000313|EMBL:CAG36120.1};
GN OrderedLocusNames=DP1391 {ECO:0000313|EMBL:CAG36120.1};
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG36120.1, ECO:0000313|Proteomes:UP000000602};
RN [1] {ECO:0000313|Proteomes:UP000000602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; CR522870; CAG36120.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6ANF4; -.
DR STRING; 177439.DP1391; -.
DR KEGG; dps:DP1391; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_039478_0_0_7; -.
DR Proteomes; UP000000602; Chromosome.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd11592; Agmatinase_PAH; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR NCBIfam; TIGR01230; agmatinase; 1.
DR PANTHER; PTHR11358:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000602}.
SQ SEQUENCE 344 AA; 37902 MW; D38E1442F7404A1B CRC64;
MKCLRAKSSR ANYKKKHFKN KSLQGKQTMS KPVNALASPR FCGIRTFMRL PYQTDLQDID
FAVLGIPFDT ATTYKPGCRF GPAGIRAAST ILKSYEEVLD VDIFEECSGV DYGDIDIIPG
HLDESFERIE EGMSALLKND IIPVVMGGDH SITLPQLRSI VKKHGPVALI HFDAHSDTGS
DYFGKPYNHG TTFHWAIKEG LIKPEESTQT GIRGPLYGRD SLKFVRESGM QVITGWELHE
IGINEAIKRI KERISPGTPV FMSFDIDFLD AAYAPGTGTP EIGGFTTHEA LKLVLNCCQG
QELVGMDLVE VLPESDNAEI TSFAAAGIMH AFLSCVAANK RAKR
//
