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Database: UniProt
Entry: A0A0G3H9T8_9CORY
LinkDB: A0A0G3H9T8_9CORY
Original site: A0A0G3H9T8_9CORY 
ID   A0A0G3H9T8_9CORY        Unreviewed;       379 AA.
AC   A0A0G3H9T8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=ATP-grasp domain {ECO:0000313|EMBL:AKK08638.1};
GN   ORFNames=CTEST_05975 {ECO:0000313|EMBL:AKK08638.1};
OS   Corynebacterium testudinoris.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK08638.1, ECO:0000313|Proteomes:UP000035540};
RN   [1] {ECO:0000313|EMBL:AKK08638.1, ECO:0000313|Proteomes:UP000035540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK08638.1,
RC   ECO:0000313|Proteomes:UP000035540};
RX   PubMed=26227591;
RA   Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT   DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL   Genome Announc. 3:e00784-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT   recovered from necrotic lesions in the mouth of a tortoise.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP011545; AKK08638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G3H9T8; -.
DR   STRING; 136857.CTEST_05975; -.
DR   KEGG; cted:CTEST_05975; -.
DR   PATRIC; fig|136857.5.peg.1187; -.
DR   Proteomes; UP000035540; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000035540}.
FT   DOMAIN          87..283
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   379 AA;  41622 MW;  FEB3D82855A8E929 CRC64;
     MWTALKILLA VEAMTIGASK LAERADELGY QLRLLAEDPS LYSDLDGVEV VIFPTRDHAA
     IRSYVDGIRD ELGGIFSPTD TWGVIAAELR EEFDLPRRHS AAQLRDLRDK QWVRRTLGEV
     AVDSFPRIIK PRGGTGSTGV TLVHNEDELA SALGSVDDAS SYVIEPYYRG PHYSAELWSN
     GTTTVFFGVT NRILTPPPLF LEKVKTFPHE HGTPWEASVE QWAREILSTL DYRVGFAHLE
     FIETAAGFEL VEINARMPGA LITPAIEACT NYDPYALIID DALNRQPELP ERREIIGGHS
     HVSLYASATG RLTSIDGLPD LKNYPGAPGW VPAKSPGDEV PDISSFRARI GNVYATANSP
     ALAQDRAIAA SQVITVEIQ
//
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