ID S0ES88_CHTCT Unreviewed; 575 AA.
AC S0ES88;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Carbamoylphosphate synthase large subunit (Split gene in MJ) {ECO:0000313|EMBL:CCW33949.1};
GN ORFNames=CCALI_00110 {ECO:0000313|EMBL:CCW33949.1};
OS Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC Chthonomonadaceae; Chthonomonas.
OX NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW33949.1, ECO:0000313|Proteomes:UP000014227};
RN [1] {ECO:0000313|Proteomes:UP000014227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23976 / ICMP 18418 / T49
RC {ECO:0000313|Proteomes:UP000014227};
RA Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT from the Armatimonadetes phylum (formally candidate division OP10).";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; HF951689; CCW33949.1; -; Genomic_DNA.
DR RefSeq; WP_016481513.1; NC_021487.1.
DR AlphaFoldDB; S0ES88; -.
DR STRING; 454171.CP488_01047; -.
DR KEGG; ccz:CCALI_00110; -.
DR PATRIC; fig|1303518.3.peg.112; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_1_0; -.
DR InParanoid; S0ES88; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000014227; Chromosome.
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 GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 3: Inferred from homology;
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}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000014227}.
FT DOMAIN 133..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 575 AA; 64065 MW; AA3A3E07D9E92A24 CRC64;
MPKDKSLKKV MVIGSGPIVI GQAAEFDYAG SQACRALREE GISVVLINSN PATIMTDSDM
ADRVYIEPLN VEFATRVIER ERPDGLLPTL GGQTGLNLAT QLAEAGILEK YGVRLLGTPL
EAIRKAEDRE EFRNLMRAIG EPVPESWIIT DEDQLSEPIS AGIWPLIVRP AYTLGGTGGG
IAHNEEELYE IAHRGLSLSM RHQVMVERYL NGWKEIEYEV MRDANDTAIT VCNMENIDPM
GVHTGDSIVV APSQTLTDKE YQMLRSASLK IIRALGIEGG CNVQLALDPK SFAYYVIEVN
PRVSRSSALA SKATGYPIAR VAAKIAIGLH LDEIENAVTR KTLACFEPAL DYCVVKIPRW
PFDKFVLADR RITTQMKATG EVMAIDRSFE AALMKAIRSL EIGIYGLTNR KSHLLSDIEL
EEAIRVPNDE RLWAITEGFR RGMLVEEIHA LSHIDPWFLR KIEGLVKLET KLRLNARAIA
RLALQEEDLG NEPTNYPLVT RLLREAKHAG FPDRVIAEFA EIPEAKLRAL RKRLGIQPVY
KMVDTCAAEF EAATPYFYSC YDQEDEALVE TTHGS
//
