ID J2Z7C9_9LACO Unreviewed; 1007 AA.
AC J2Z7C9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Carbamoyl-phosphate synthase pyrimidine-specific large chain {ECO:0000313|EMBL:EJN56483.1};
GN ORFNames=A11Y_117886 {ECO:0000313|EMBL:EJN56483.1};
OS Loigolactobacillus coryniformis subsp. coryniformis CECT 5711.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN56483.1, ECO:0000313|Proteomes:UP000007271};
RN [1] {ECO:0000313|EMBL:EJN56483.1, ECO:0000313|Proteomes:UP000007271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271};
RA Rodriguez J.M.;
RT "Complete Genome Sequence of Lactobacillus coryniformis CECT5711.";
RL Submitted (MAY-2012) 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 -!- 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:EJN56483.1}.
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DR EMBL; AKFP01000007; EJN56483.1; -; Genomic_DNA.
DR RefSeq; WP_004562523.1; NZ_AKFP01000007.1.
DR AlphaFoldDB; J2Z7C9; -.
DR STRING; 1185325.A11Y_117886; -.
DR PATRIC; fig|1185325.3.peg.464; -.
DR Proteomes; UP000007271; 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 Reference proteome {ECO:0000313|Proteomes:UP000007271};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 659..848
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1007 AA; 107855 MW; 14DC49307C528F7D CRC64;
MPKLTNIHKI AVIGSGPIVI GQAAEFDYAG SQACLSLKEE GYQVVLINSN PATIMTDDEI
ADKVYLEPLT LESVSAILAK ERPDALLPTL GGQTGLNLAV ELDDAGILAK YNIQLLGTGL
ATIKQAEDRE SFKELMQKIG QPIPASKTVH AVQAALDFAH EIGYPVIVRP AYTLGGTGGG
IAADAAELQK IMVRGLSMSP ANECLIEKSI AGFKEIEYEV MRDNLGDKIT VCNMENFDPV
GIHTGDSIVF APSQTLNDTE YQTLRQASLD IIDALDIKGG CNVQLAQDPN SEHYYVIEVN
PRVSRSSALA SKATGYPIAK IAAKIAVGLN LSELRNPVTK TTYAAFEPAL DYVVAKIPRF
PFDKFNTAER KLGTQMKATG EVMGIGSTIE ESLLKALQSM EIDQTAINQL KPSAATPDLA
AALHTPTDDR LLVIFAALRV GYSVDKIQVL TQIDRLFLDK LAHIVTLQQQ LAQDLTANYA
TAKKFGFNDA MISAVTTEPL PGSAPVYKMV DTCAGEFASS TPYFYSTYFG SENESQPLGN
SILVIGSGPI RIGQGVEFDY TTVHCVQAIQ QAGYHAIIVN NNPETVSTDF SISDKLYFEP
LTLESVLHIA ELEQPLGVIV QFGGQTAINL TAGLVANGLK ILGTSLHGIE QTEDRHQFEA
LLQHLNVNQP AGNTATSLAA ASKIAAKIGY PVMVRPSFVL GGRAMAIVHD ETELAHYLTN
ALHAAPEQPI LIDHYVQGLE CEVDILSDGY NVFIPGIMEH IEGAGIHSGD SIAVYPPQRL
TVAQQAEIVS IATKIGQNVH CIGMMNIQFI VADQVYVIEV NPRASRTVPF MSKVTKLHLA
KIATRLILGA SFAELGLTPG LLTPPNLVAI KAPVFSFTKL PGISTVLSPE MKSTGESIGI
ATDYTTALGK ALTDSYHFHG SHAGQFVLLT PTMAADTTVL QEIAHAQLVP QVLSADTVPD
VAAEQVALVA NTNDHQTAAD PLNYFALSQN IPLFTAKDTL LAALTVN
//
