ID A0A328VJ47_9CHLR Unreviewed; 381 AA.
AC A0A328VJ47;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:RAQ94285.1};
GN ORFNames=A4R35_01995 {ECO:0000313|EMBL:RAQ94285.1};
OS Thermogemmatispora tikiterensis.
OC Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC Thermogemmatisporaceae; Thermogemmatispora.
OX NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ94285.1, ECO:0000313|Proteomes:UP000248706};
RN [1] {ECO:0000313|EMBL:RAQ94285.1, ECO:0000313|Proteomes:UP000248706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T81 {ECO:0000313|EMBL:RAQ94285.1,
RC ECO:0000313|Proteomes:UP000248706};
RA Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA Levin D.B.;
RT "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT Carbohydrate Degradation Ability.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:RAQ94285.1}.
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DR EMBL; MCIF01000002; RAQ94285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328VJ47; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000248706; Unassembled WGS sequence.
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 CDD; cd09990; Agmatinase-like; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR11358:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR Pfam; PF00491; 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:UP000248706}.
SQ SEQUENCE 381 AA; 41623 MW; 5133F4D16131027C CRC64;
MSIFHNHGLS HRESKDASFS REDFEGYSAA QAEAKLPQAR SEAEISRAIA LGLEAAQSIE
DRTISCFSRG ELPHWAGINT FLKMPFLENV HEVDQYDIAI LGVPFDIGTT YRPGTRFGPQ
AIRRISALYT TYNYELGVDL REQVKICDLG DVFTVANIEK SFDQISKAVS FVLSKGTMPI
ILGGDHAIGY PCLRGIAENI EGNVGIIHLD RHVDTQEKDM DERMHTTPWF HATNIPNAPP
ANLVQIGIGG WQVPRAGVAV ARERGTTILT ITDVERLGIE KVAEIALEVA WKGAKAVYLS
FDIDSLDAGF VPGTGWPEPG GFLPREALKL LQLVAREGVC GMEVVEVSPP YDISDTTALM
AVRAIVDVIA TMVLHGKIGG R
//
