ID K8DZ14_9FIRM Unreviewed; 291 AA.
AC K8DZ14;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:CCO08237.1};
DE EC=3.5.3.11 {ECO:0000313|EMBL:CCO08237.1};
GN Name=speB {ECO:0000313|EMBL:CCO08237.1};
GN ORFNames=DESHY_20106 {ECO:0000313|EMBL:CCO08237.1};
OS Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO08237.1, ECO:0000313|Proteomes:UP000009315};
RN [1] {ECO:0000313|EMBL:CCO08237.1, ECO:0000313|Proteomes:UP000009315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT hydrothermale Lam5(T).";
RL Genome Announc. 1:e00114-e00112(2013).
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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:CCO08237.1}.
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DR EMBL; CAOS01000009; CCO08237.1; -; Genomic_DNA.
DR RefSeq; WP_008411558.1; NZ_FQXF01000016.1.
DR AlphaFoldDB; K8DZ14; -.
DR STRING; 1121428.DESHY_20106; -.
DR eggNOG; COG0010; Bacteria.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000009315; Unassembled WGS sequence.
DR GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd11593; Agmatinase-like_2; 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:SF43; AGMATINASE; 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:UP000009315}.
SQ SEQUENCE 291 AA; 31643 MW; 3AE246C922F843C7 CRC64;
MFNLLDAGSG FLGASRDYRN AGVVLVGAPM DFTVSFRPGT RQGPQAIRQV SVGLEEYSVM
LDRDLADYNY YDAGDVSLPF GHVTESLRRI GQVVNGILKD DKFPLVLGGE HLISLPVIEQ
VAAKYPGLKI LHFDAHADLR EDYMGQALSH ASVIRRAADL VGGKNIYQFG IRSGTRDEFV
YAKQNTHMFV GKVLEPLKQV LPELAGHPVH ITLDIDVVDP AFAPGTGTPE PGGCSAAEIL
EALYALRDLR VVGFDLVEIS PAYDHSERTA ILGAKLVREA ILAFGKPEKQ S
//
