ID A0A0R1Q4M4_9LACO Unreviewed; 1014 AA.
AC A0A0R1Q4M4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:KRL39441.1};
GN ORFNames=FD01_GL002547 {ECO:0000313|EMBL:KRL39441.1};
OS Lacticaseibacillus manihotivorans DSM 13343 = JCM 12514.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423769 {ECO:0000313|EMBL:KRL39441.1, ECO:0000313|Proteomes:UP000051790};
RN [1] {ECO:0000313|EMBL:KRL39441.1, ECO:0000313|Proteomes:UP000051790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13343 {ECO:0000313|EMBL:KRL39441.1,
RC ECO:0000313|Proteomes:UP000051790};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:KRL39441.1}.
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DR EMBL; AZEU01000295; KRL39441.1; -; Genomic_DNA.
DR RefSeq; WP_056964992.1; NZ_AZEU01000295.1.
DR AlphaFoldDB; A0A0R1Q4M4; -.
DR PATRIC; fig|1423769.4.peg.2749; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000051790; 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:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 2.
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; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000051790};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 668..857
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1014 AA; 108688 MW; A3BEB87C0898572F CRC64;
MPKNLNIHKI VVIGSGPIIV GQAAEFDYSG SQACLSLREE GYSVVLINSN PATIMTDDDI
ADKIYLEPLT LESVTHILEV EKPDALLPTL GGQTGLNMAV ALDEAGVLKR LNIQLLGTGL
DTIHQAEDRQ AFKQLMEDLH QPVPQSLTVH DLGSALKFAD ACGYPVIVRP AFTLGGTGGG
IAHDEAELKI IGQRGLELSP NTECLIEKSI AGYKEIEFEV MRDAAGTTIS VCCMENVDPV
GIHTGDSIVV APNQTLDDPT FQKLRSASLQ IVDALNIQGG CNVQLAQDPN SDQYYIIEVN
PRVSRSSALA SKATGYPIAK IAAKIAVGLN LQEIQNPVTK TTFAAFEPTL DYVVAKIPRF
PFDKFVSAER QLGTQMKATG EVMGIGTTFE EALLKAVQSL ELDTKMQTTL LPKTTPTESE
LTEALEHPTD VRLFYLFEAL RQGWSKQKIQ AHTQITMFFL NKLAHIFNTL TGLQTGQLTV
AKAHAANQLG FTAGMIAQAA GVSDSVVNAL LPAPVYKMVD TCAGEFASET PYFYSTAFPG
ENESKPLGNS IIVIGSGPIR IGQGVEFDYT TVHCVQAIQA AGYHAIIINN NPETVSTDFS
ISDKLYFEPL TAESVMHIVD LEKPLGVIVQ FGGQTAINLT AKLAKLGVKI LGTSLAGINQ
TENRHEFETL LADLHINQPQ GDTAMNLEEA RQIAPVVGYP VMVRPSYVLG GRAMAIVEDE
SELAEYVQKA IAAAPHQPIL IDHDVQGLEC EVDILSDGQD VFIPGIMEHL EGSGIHSGDS
IAIYPPQHLT AAQQAEIIQT ATAIGKAVHC VGMMNVQFIV ADQLYVIDVN PRASRTVPFM
SKVTGYPLAK LATNLILGKT LADLNLPIGC PTPKPGVAIK APVFSFTKLP GMVTGLAPEM
KSTGETIGLG RDYHEALAKA LCDSYHCTLP KAGDVLLSSH QPNAELASEL ANVGVKLTLG
DGQIPAQKPW AVLNLDEHQT TASPLNYYAL SHQVPLLTST ATLTGLLEAV LQPA
//
