ID H1LIH5_9LACO Unreviewed; 1022 AA.
AC H1LIH5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EHO49765.1};
GN ORFNames=HMPREF9104_02416 {ECO:0000313|EMBL:EHO49765.1};
OS Lentilactobacillus kisonensis F0435.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=797516 {ECO:0000313|EMBL:EHO49765.1, ECO:0000313|Proteomes:UP000005025};
RN [1] {ECO:0000313|EMBL:EHO49765.1, ECO:0000313|Proteomes:UP000005025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0435 {ECO:0000313|EMBL:EHO49765.1,
RC ECO:0000313|Proteomes:UP000005025};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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:EHO49765.1}.
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DR EMBL; AGRJ01000210; EHO49765.1; -; Genomic_DNA.
DR RefSeq; WP_008857571.1; NZ_JH591048.1.
DR AlphaFoldDB; H1LIH5; -.
DR STRING; 797516.HMPREF9104_02416; -.
DR PATRIC; fig|797516.3.peg.2166; -.
DR HOGENOM; CLU_000513_1_0_9; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000005025; 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..863
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1022 AA; 111589 MW; EBEBD9D932CE93FF CRC64;
MPKRTDINKI VIIGSGPIVI GQAAEFDYAG SQACLSLREE GYEVILVNSN PATIMTDDEI
ADKVYLEPLT VPSLKKILIK EHPDAILPTL GGQTGLNLAV ELSKDGILDK LNIELLGTSL
KTINQAEDRE QFKDLMEELH QPIPASKTVY DLETGIKFAH QIAYPVIIRP AYTLGGTGGG
IAHNDAEMTT ILNRGLTMSP STECLVEKSI AGYKEIEFEV MRDHHGSSII VTGMENFDPV
GVHTGDSIVF APTQTLTDKE YQRLRDASLT IVNALKIEGG CNVQLAQDPF SENYYVIEVN
PRVSRSSALA SKATGYPIAK IAAKIAVGLN LDEIINPITQ TTFAMFEPAL DYVVAKIPRF
AFDKFTNADR KLGTQMKATG EVMAIGSTIE ESLLKAVQSL ELDKQAQVDL IPEYTKGMSL
GDLLEKIKTP TDYRLFELFA AIGKGATIQQ INRATQIDMY FLSKLEAIIK MQQKLSDGLL
CADLVLDARK LGFNNTMIEA IRSTTDHELE KLSNMEDQHL VYKMVDTCAA EFESTTPYYY
STIGHENESK PLGNSIVVIG AGPIRIGQGV EFDYATVHCV KAIQTAGYNA IIINNNPETV
STDFSISDKL YFEPLDIDSV MNVINLEKPI GVIVEFGGQT AINLTEALTE HGVSILGTSL
HGIEQTENRH EFENLLIDQD IDHPKGDTAT TIAEAQEIAH RLGFPVLVRP SFVLGGKGMA
VVHDEDELNE YLVPALKASH GEPLLIDQYI HGIECEVDIL SDGQQVFVPG IMEHLEGSGI
HSGDSIAMYP PQHLSADTKD QIVAIATKIG EQVHAVGMMN IQFIAANDTV YVIEVNPRAS
RTVPFMSKIT KRHLAQLATQ LILGKSLEDL GLIPGLNPEP AKVYVKAPVF SFAKLPGAPT
ALSPEMKSTG EDIGSGDTLQ AAMHNALFDS YHIDTNDLNG VVLISEFDAN DDHVASKLKS
AGFEVQAYQP DMDWPEKIAF VLSSEDETDD EKQLVANALS HQVPVFTAQD TVLGIFQPQL
IK
//
