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Database: UniProt
Entry: A0A0F0KRT7_9MICO
LinkDB: A0A0F0KRT7_9MICO
Original site: A0A0F0KRT7_9MICO 
ID   A0A0F0KRT7_9MICO        Unreviewed;       329 AA.
AC   A0A0F0KRT7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:KJL23632.1};
DE            EC=6.3.5.5 {ECO:0000313|EMBL:KJL23632.1};
GN   Name=carB_1 {ECO:0000313|EMBL:KJL23632.1};
GN   ORFNames=RN50_00970 {ECO:0000313|EMBL:KJL23632.1};
OS   Microbacterium foliorum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL23632.1, ECO:0000313|Proteomes:UP000033572};
RN   [1] {ECO:0000313|EMBL:KJL23632.1, ECO:0000313|Proteomes:UP000033572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL23632.1,
RC   ECO:0000313|Proteomes:UP000033572};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJL23632.1}.
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DR   EMBL; JYIU01000035; KJL23632.1; -; Genomic_DNA.
DR   RefSeq; WP_045253386.1; NZ_JYIU01000035.1.
DR   AlphaFoldDB; A0A0F0KRT7; -.
DR   KEGG; mfol:DXT68_04420; -.
DR   PATRIC; fig|104336.4.peg.994; -.
DR   Proteomes; UP000033572; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR   PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR   Pfam; PF15632; ATPgrasp_Ter; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KJL23632.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000033572}.
FT   DOMAIN          114..288
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   329 AA;  34795 MW;  3A5771A87F602A8B CRC64;
     MTARVLVTGA GGPAGVAVIR SLLRRSDLEV FAADMDGWAS GIYLVPASHR RLVPPGRDED
     FVPAITRMVA DDRLDLVIST VDVELIALAG RRDELAPAVL AAPSQDTLSV ALDKMLLAER
     CAPTGLTPRT VLAGPDAQAV DWEFPVFAKP RQGAGSRGIR LVPDRAALDE LPTDEGLIVQ
     DFLPGEEYSV DVIADASGAV VAAVPRTRAR VDSGVAIAGR TVHDAELEDA AAEIARAIGL
     VGVANVQLRR DRAGRAVLLE VNPRFPGALP LTIAAGVDIP SLVADLFLGR DLPATVAFRE
     VASVRYLEDI IVEVDDILIS DHAGHQEEL
//
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