ID A0A1E4JL59_9PROT Unreviewed; 648 AA.
AC A0A1E4JL59;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:ODU26268.1};
DE Flags: Fragment;
GN ORFNames=ABS93_03955 {ECO:0000313|EMBL:ODU26268.1};
OS Thiobacillus sp. SCN 62-729.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660148 {ECO:0000313|EMBL:ODU26268.1, ECO:0000313|Proteomes:UP000094151};
RN [1] {ECO:0000313|EMBL:ODU26268.1, ECO:0000313|Proteomes:UP000094151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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}.
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:ODU26268.1}.
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DR EMBL; MEFL01000068; ODU26268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4JL59; -.
DR Proteomes; UP000094151; 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 GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 2.
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; IPR006275; CarbamoylP_synth_lsu.
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 NCBIfam; TIGR01369; CPSaseII_lrg; 1.
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; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}.
FT DOMAIN 133..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 648
FT /evidence="ECO:0000313|EMBL:ODU26268.1"
SQ SEQUENCE 648 AA; 71331 MW; E7ADBE6AF7EF5E1C CRC64;
MPKRTDLKSI LIIGAGPIVI GQACEFDYSG AQACKALREE GYKVILVNSN PATIMTDPDM
ADVTYIEPIS WQVVEKIIEQ ERPDALLPTM GGQTALNCAL DLARHGVLEK YGVEMIGASK
EAIDKAEDRE KFKAAMTRLG LGSARSSIAH SMEEALQVQA ALGFPTIIRP SFTMGGSGGG
IAYNKDEFVA ICERGLEASP THELLIEESL LGWKEYEMEV VRDHKDNCII ICSIENFDPM
GVHTGDSITV APAQTLTDKE YQIMRNASLA VLREIGVDTG GSNVQFSINP EDGRMVVIEM
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELQNEIT GGATPASFEP SIDYVVTKIP
RFAFEKFPQA DDRLTTQMKS VGEVMAMGRS FQESLQKALR GLEVGADGFD PRTTDQEEIE
AELMSPGPER IWYVGDAFRV GMSLEEIHAV SKIDPWFLDQ IQGLIELEAS LSGRALTDLG
RDELRRLKRA GFSDRRLAKL LSTDQHAVRA RRNELALHPV YKRVDTCAAE FATQTAYMYS
TYEEECEAHP TDARKIMVLG GGPNRIGQGI EFDYCCVHAA LALRENGFET IMVNCNPETV
STDYDTSDRL YFEPLTLEDV LEIVRIEKPF GVIVQYGGQT PLKLARDL
//
