ID   Q2MF09_STRSD            Unreviewed;       410 AA.
AC   Q2MF09;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative carbamoyl-phosphate synthase, TobL {ECO:0000313|EMBL:CAH18563.1};
GN   Name=tobL {ECO:0000313|EMBL:CAH18563.1};
OS   Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 /
OS   CBS 697.72 / NBRC 16175 / NCIMB 11028 / NRRL B-12390 / A12253. 1)
OS   (Streptomyces tenebrarius).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Streptoalloteichus.
OX   NCBI_TaxID=1933 {ECO:0000313|EMBL:CAH18563.1};
RN   [1] {ECO:0000313|EMBL:CAH18563.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain: DSM 40477 {ECO:0000313|EMBL:CAH18563.1};
RA   Aboshanab K., Schmidt-Beissner H., Wehmeier U., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Comparison of the gene clusters for the biosynthesis of the aminoglycoside
RT   antibiotics tobramycin-apramycin (Streptomyces tenebrarius DSM 40477), and
RT   hygromycin B (Streptomyces hygroscopicus subsp. hygroscopicus DSM 40578).";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AJ810851; CAH18563.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MF09; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR041472; BL00235/CARNS1_N.
DR   InterPro; IPR040570; LAL_C2.
DR   PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR   PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR   Pfam; PF13535; ATP-grasp_4; 1.
DR   Pfam; PF18130; ATPgrasp_N; 1.
DR   Pfam; PF18603; LAL_C2; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Helicase {ECO:0000313|EMBL:CAH18563.1};
KW   Hydrolase {ECO:0000313|EMBL:CAH18563.1};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          117..314
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   410 AA;  43707 MW;  354E5CDECAB76B5B CRC64;
     MNNELVVFVN VRRTHLERGA VFEAAHRLGY GVALLADAVP EGLPRGIVRT VVRLDTRDEA
     AVHAAVDEIA AEHRIAAVLG WSERDVTTVS GIAQRLGLPG VSPGAARLAR NKYLMREAVA
     EHHPHLVPRF ARVTDWSDLS RAVELVGFPA VLKPTSSSGS RGIFVIDGPA GLRPAFDRLM
     DLTATTETRH ELIYEEFLHG TEHSVEGFVH CGQIHVVGVI DKRTTEPFRL ELAHLHPSAL
     PADRLDAVHR LTADVVSALG LDDCAFHLEC MVAPDGGVRL VEIGARGGGD FIASHLVGLA
     TGRSFVENAI RVATGRPPLD AAGPPLWACV RKILTDRVGT LTGYAGLDDA CRVPGVRHLV
     IEQPVGAEIT QPPVDFKSCI LGAVITVGDS AEAAEGSAEQ AAALVRADIS
//