ID D9VWK8_9ACTN Unreviewed; 320 AA.
AC D9VWK8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Formimidoylglutamase {ECO:0000313|EMBL:EFL15218.1};
GN ORFNames=SSNG_02470 {ECO:0000313|EMBL:EFL15218.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL15218.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL15218.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL15218.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; GG657750; EFL15218.1; -; Genomic_DNA.
DR RefSeq; WP_007264163.1; NZ_GG657750.1.
DR AlphaFoldDB; D9VWK8; -.
DR STRING; 253839.SSNG_02470; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_039478_0_0_11; -.
DR Proteomes; UP000005763; 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 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}.
SQ SEQUENCE 320 AA; 34060 MW; 860F7AE9A4BC5579 CRC64;
MSTQPRGPVD SSRIPRYAGP ATFARLPRLD EVGSADVAVV GVPFDSGVSY RPGARFGGNA
IREASRLLRP YNPAQDASPF ALAQVADAGD IAVNPFNINE AVETVEAAAD ELLGNGSRLM
TLGGDHTIAL PLLRSVAKKH GPVALLHFDA HLDTWDTYFG AEYTHGTPFR RAVEEGILDT
EALSHVGTRG PLYGKQDLDD DAKMGFGIVT SADVYRRGAD EVADQLRQRI GDRPLYISID
IDVLDPAHAP GTGTPEAGGM TSRELLEIIR GLSSCNLVSA DVVEVAPAYD HAEITSVAAS
HTAYELTTIM SRQIAASRQG
//
