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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//