ID A0A011V5T5_RUMAL Unreviewed; 425 AA.
AC A0A011V5T5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Carbamoyl-phosphate-synthetase {ECO:0000313|EMBL:EXM40877.1};
GN ORFNames=RASY3_04180 {ECO:0000313|EMBL:EXM40877.1};
OS Ruminococcus albus SY3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1341156 {ECO:0000313|EMBL:EXM40877.1, ECO:0000313|Proteomes:UP000021369};
RN [1] {ECO:0000313|EMBL:EXM40877.1, ECO:0000313|Proteomes:UP000021369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY3 {ECO:0000313|EMBL:EXM40877.1,
RC ECO:0000313|Proteomes:UP000021369};
RA Dassa B., Borovok I., Lamed R., Flint H., Yeoman C.J., White B.,
RA Bayer E.A.;
RT "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT comparative genome-wide analysis of six Ruminococcal strains.";
RL Submitted (JUN-2013) 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:EXM40877.1}.
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; JEOB01000001; EXM40877.1; -; Genomic_DNA.
DR RefSeq; WP_037285282.1; NZ_JEOB01000001.1.
DR AlphaFoldDB; A0A011V5T5; -.
DR PATRIC; fig|1341156.4.peg.550; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000021369; Unassembled WGS sequence.
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; 3.40.50.20; -; 1.
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; IPR016185; PreATP-grasp_dom_sf.
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 SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 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:UP000021369}.
FT DOMAIN 106..308
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 425 AA; 47655 MW; EDCBC540DF0F2AE1 CRC64;
MDLKGKRLLI LGATTVEIEI INEAKKLGVY TIVTDNHTDW SLAPAKYVAD EAYDLSWSDM
DALEKLCRER NVDGCLAGYS ERRVECLTEL CKRMGFYCYT EGADLGTIFS KDKFREACIN
AGIPATSAYD IHDENISFPV IVKPVDNAGS RGVSVCKDRE ELNKAYENAC KSSISGRAII
EEFLDGDDPR YEPVFFYTIH NGTATLSNSL DRIMVDFGFG EGIIKQAVGN VYPSRYLESF
IEKQDAQYRE LFRSLGMKNG YALMQGKMKN GNFVTVDLGY RLEGSLTFHY SDFINGMNVI
QMMIRHALTG TMGDDSIINE KDDPRLDKTG VTLTLLATKG TIASISGLDE IKNEKCVIYV
CPKMKVGTVC KLPADYSQVF ARIYMCSDDK QELRDTIEKI YSTVKVLDEE GNNMLIGRYD
ADELK
//
