ID   Q03S50_LEVBA            Unreviewed;       858 AA.
AC   Q03S50;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Carbamoylphosphate synthase large subunit {ECO:0000313|EMBL:ABJ63972.1};
GN   OrderedLocusNames=LVIS_0829 {ECO:0000313|EMBL:ABJ63972.1};
OS   Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS   1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=387344 {ECO:0000313|EMBL:ABJ63972.1, ECO:0000313|Proteomes:UP000001652};
RN   [1] {ECO:0000313|EMBL:ABJ63972.1, ECO:0000313|Proteomes:UP000001652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 /
RC   NCIMB 947 / NCTC 947 {ECO:0000313|Proteomes:UP000001652};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
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DR   EMBL; CP000416; ABJ63972.1; -; Genomic_DNA.
DR   RefSeq; WP_011667758.1; NC_008497.1.
DR   AlphaFoldDB; Q03S50; -.
DR   STRING; 387344.LVIS_0829; -.
DR   KEGG; lbr:LVIS_0829; -.
DR   PATRIC; fig|387344.15.peg.801; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_1_9; -.
DR   Proteomes; UP000001652; 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: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; 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; 2.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 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   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:UP000001652};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          133..327
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   858 AA;  94617 MW;  0B66309BAE62A35B CRC64;
     MPSLNDIQKV LIIGGGPTEI GHETELDSAT VQIMTEFKKH GVRTLIIDNN PFSVALEEIQ
     PTNMYVQAVT TENVRHIIEK DQPDAILPSL GGLLGIQIAQ ELIEDGDIGR FGVTVLGMAP
     ATLRQINNPA ALNATLKEIQ EPIIEAQVVS TTDEAMGMVE AIGFPLIVKP VSPRVDTNRT
     ICENVDDMLT ALNQGFQQSR FDQCSLERSV VGYKEVEMVA VRDVADTKIL ICGLENIDPI
     GIHSGDSIVV TPPQTLNDRE YQDLRDATFR IATELGIVGV LHLHFALNPA NQHFYVTKIA
     PYFTRGVALA ARTTGYPIAL VVGALLLGQR LVDVKLPGGY VKQTAIMEPM VDHVGVRIPL
     WPFQEVPDAD QHLDTVMKAV GSTIGLGRSV EEALLKSVRS SQFSPRDVLP SVSNLTDGEM
     IRQLIHPLAN RILVLIEALR RGYSPAELSE LTKIDNFYFV KLQHLLLIEQ AIKDHPLDVD
     VLQRARYFGF GDGMIARIWQ TDTAKIRQLL ADARIAPTYK MIEPTAGEFP EKTSGFYSTF
     EYENESQSLG ERTALVLGRG GNQLGPNSAA EYFTTEMLKQ LKRAGYHTIL MNTNPNAVAI
     APEFSDKQYV DPIQLGDVLN VIHVEHPDIV IVPGNRHYLT RELSKLDINL HVLPPDQETD
     QPAPEMATIG VSLFVHNQHK LAVGVMDMIA PGMNKALSQV TAFRMPAELP RSRRTNLVEQ
     AKQAVSERQV TGMVQVLFAP KPDSDSHQLT VVGVRPSRLT EMAFLSKVTG VNWVRMLTRQ
     HIGTLDDAEL SAIKVDIHSN RVALMNAAFP FRQLHVLNRP GTTDQEVGAT IAFGSSEALT
     LTNLSDTDEL DRIINRTI
//