ID A0A0R1YTF3_9LACO Unreviewed; 1021 AA.
AC A0A0R1YTF3;
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:KRM45808.1};
GN ORFNames=FC51_GL000721 {ECO:0000313|EMBL:KRM45808.1};
OS Lentilactobacillus parabuchneri DSM 5707 = NBRC 107865.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423784 {ECO:0000313|EMBL:KRM45808.1, ECO:0000313|Proteomes:UP000051957};
RN [1] {ECO:0000313|EMBL:KRM45808.1, ECO:0000313|Proteomes:UP000051957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5707 {ECO:0000313|EMBL:KRM45808.1,
RC ECO:0000313|Proteomes:UP000051957};
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:KRM45808.1}.
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DR EMBL; AZGK01000013; KRM45808.1; -; Genomic_DNA.
DR RefSeq; WP_057911293.1; NZ_AZGK01000013.1.
DR AlphaFoldDB; A0A0R1YTF3; -.
DR PATRIC; fig|1423784.4.peg.725; -.
DR Proteomes; UP000051957; 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; 2.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 673..862
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1021 AA; 111462 MW; 63809C3AC3B05639 CRC64;
MPKREDIKKV LIIGSGPIVI GQAAEFDYAG SQACLSLREE GYSVILVNSN PATIMTDDEI
ADKIYLEPLT VPSLKKIIEK EHPDAILPTL GGQTGLNLAV ELSKDGILDK LGIELLGTSL
QTINEAEDRE KFKDLMQELH QPIPDSKTVY DLQDGLDFAH QIDYPVIIRP AYTLGGTGGG
IAHNDDEMKT ILNRGLTMSP STECLIEKSI AGYKEIEFEV MRDHHGSSII VTGMENFDPV
GIHTGDSIVF APTQTLTDKE YQRLRDASLT IVNALKIEGG CNVQLAQDPN SEAYYVIEVN
PRVSRSSALA SKATGYPIAK IAAKIAIGLN LDEIMNPITQ TTFAMFEPAL DYVVAKIPRF
AFDKFTNADR KLGTQMKATG EVMAIGSTIE ESLLKAVQSL ELDQQAQTDL IPTYTRDMSM
GDLLEKIKTP TDYRLFEIFA AIGKGATIQQ INRSTQIDLY FLSKLENILK MQQQMTDGLL
SADMVLKARK LGFNNTMIKA IHHATDDELV KLDQMEDQHL VYKMVDTCAA EFESTTPYYY
STVGNENESK PLGNSIVVIG AGPIRIGQGV EFDYATVHCV KAIQAAGYNA IIINNNPETV
STDFSISDKL YFEPLTIDSV MNIINLEQPI GVIVEFGGQT AINLTEALTK HGVSILGTSL
HGIEQTEDRH QFEDLLIDQN IAHPKGDTAT SAPESLEIAN KLGYPVLVRP SFVLGGKGMA
VVHNDDELNE YLIPALKNSH GEPILIDQYI PGTECEVDIL SDGNEVFVPG IMEHLEGAGI
HSGDSIAMYP PQTLTDDQKE KIVAIATKIG KQVHAVGMMN IQFIVADEVY VIEVNPRASR
TVPFMSKIAK LHLAQLATQL ILGKSLDEIG LKPGLHPEPA KVYVKAPVFS FAKIPGAPTA
LSPEMKSTGE DIGSGDSLQV ALHNALFDSY HIDTNNLSGD VLLSEFDANN ASLVGQLKGS
GFGIQTYHEN MDWPDDLAFV LSSEDETSDQ KQLVANALSH QVPVFTAQDT VMGVFQPQLI
K
//
