ID A0A0R1M3G4_9LACO Unreviewed; 1026 AA.
AC A0A0R1M3G4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Carbamoyl-phosphate synthase, glutamine-hydrolyzing {ECO:0000313|EMBL:KRK99812.1};
GN ORFNames=FD04_GL002173 {ECO:0000313|EMBL:KRK99812.1};
OS Secundilactobacillus odoratitofui DSM 19909 = JCM 15043.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1423776 {ECO:0000313|EMBL:KRK99812.1, ECO:0000313|Proteomes:UP000051160};
RN [1] {ECO:0000313|EMBL:KRK99812.1, ECO:0000313|Proteomes:UP000051160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19909 {ECO:0000313|EMBL:KRK99812.1,
RC ECO:0000313|Proteomes:UP000051160};
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:KRK99812.1}.
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DR EMBL; AZEE01000002; KRK99812.1; -; Genomic_DNA.
DR RefSeq; WP_056946307.1; NZ_AZEE01000002.1.
DR AlphaFoldDB; A0A0R1M3G4; -.
DR STRING; 1423776.FD04_GL002173; -.
DR PATRIC; fig|1423776.4.peg.2200; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000051160; 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 1026 AA; 111395 MW; 1ACAF84BD03E29E1 CRC64;
MPKRTDLNKI VIIGSGPIVI GQAAEFDYAG SQACLSLKEE GYETVLINSN PATIMTDDEI
ADKVYLEPLT IESVTAILKK EQPDAILPTL GGQTGLNLAV ELAKTGILDE LNIELLGTNL
HTINQAEDRE EFKALMNDLS QPIPPSKTVY DLQTGLDFAH EIGYPVIIRP AYTLGGTGGG
FANNDDEMTT VLNRGLTMSP ETECLIEKSI AGYKEIEFEV MRDHNGSSII VTGMENFDPV
GVHTGDSIVF APTQTLTDKE YQRLRDASLT IVNALKIEGG CNVQLAQDPY SEAYYVIEVN
PRVSRSSALA SKATGYPIAK IAAKIAVGLN LDEIINPITQ TTYAMFEPAL DYVVAKIPRF
AFDKFYNADR TLGTQMKATG EVMAIGSNIE ESLLKAVQSL ELDAHMQNTL LPEDAEGKSL
ADLLATIPVD TDIRLFELFA AIAKGATLEQ LHDATKIDEF FLIKLMNIMA MQKQLMTGML
TADLVLKAQK LGFDDAMIKS VCQVTDHELD QLHGMADQKL VYKMVDTCAA EFESFTPYFY
NTVGTENESK PLGNSIIVLG AGPIRIGQGV EFDYTTVHSV KAIQSAGYNA IIINNNPETV
STDFSISDKL YFEPLTIDSV MNIINLEQPL GVIVQFGGQT AINLTQQLTD RGVKILGTNM
AGINQTENRH EFEELLIDQN IAHPQGHTAM SMVEAHHIAA TLGYPVLVRP SFVLGGKGMA
IVHNQDELND YLVPALKHSG GQPILVDKYI MGTECEVDIL SDGQQVFIPG IMEHLEGAGV
HSGDSIAMYP PQHLTAAQKS EIVEIATKIG KSVHCIGMMN IQFIVADQVY VIEVNPRASR
TVPFMSKITH KHLAQLATQL IIGKSLADIN LNPGLFPEPA SVYVKAPVFS FAKLPGAPTA
LSPEMKSTGE DLGHGATLAE ALHKAFFDSY HFDSHTKGNI LVTPLDAENT DLMAALDAGG
YPHQVYQLDQ AWPDELAFVL ATEDESDLAK QLTTRALSHE VTLFTASDTV AALVSVPHSA
NARQAG
//
