ID C7XUH5_9LACO Unreviewed; 834 AA.
AC C7XUH5;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Carbamoyl-phosphate synthetase, large subunit, oligomerization domain protein {ECO:0000313|EMBL:EEU30936.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EEU30936.1};
GN Name=carB {ECO:0000313|EMBL:EEU30936.1};
GN ORFNames=HMPREF0501_00341 {ECO:0000313|EMBL:EEU30936.1};
OS Limosilactobacillus coleohominis 101-4-CHN.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=575594 {ECO:0000313|EMBL:EEU30936.1, ECO:0000313|Proteomes:UP000003987};
RN [1] {ECO:0000313|EMBL:EEU30936.1, ECO:0000313|Proteomes:UP000003987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=101-4-CHN {ECO:0000313|EMBL:EEU30936.1,
RC ECO:0000313|Proteomes:UP000003987};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Liu Y., Xu Q., Lander E., Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Lactobacillus coleohominis strain 101-4-CHN.";
RL Submitted (JUN-2009) 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}.
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DR EMBL; GG698802; EEU30936.1; -; Genomic_DNA.
DR AlphaFoldDB; C7XUH5; -.
DR STRING; 575594.HMPREF0501_00341; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_1_9; -.
DR Proteomes; UP000003987; 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; 1.
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; 1.
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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EEU30936.1};
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:UP000003987};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 132..326
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 834 AA; 93371 MW; 5F606DF889CEB66A CRC64;
MAESKPTALI IGAGSDNLQQ GGELDYATLE VGKTLQKAGF ETVLVDDNPF STSLDTTSAI
TQRYILPLTA QSIIDVINQR HPQLIVPTLG GRRAFEILQT VGESGILTEN DIRIAGVPEA
TVRQVNNPML LNQTLRRLQA PTKKIATVDN YQAALEMARA VGFPVVVRAV FPKSLRMRRI
VQDSEELRTA VSRGIQMSRS GQVMVQQSLA GLKEIEVMVM RDSSGNMMCL GIAEDIDPIG
IHAGDSITVL PAQTLLDRNI QDMRNTAFAI TRKLRIVGIN HVQFAFDPHQ NRYYVIKNSP
YFDRISTFTE IATGYPVSRV VGHLYAGELL RNIRLDHGLT KHTAVTEPVM DRTAVRMPVF
PFSQLTVNNQ KLGTQKKSVG STIGIGRSLI EALLKANADY QFGWHNGQAK LMHGISDDQL
DQLLIHPHGD RLYSLIEAIR RGYSEKELAE LTKIDRYYLA QFNRLLKIQT EIRQLKESPA
VLKEAKYWGF DDGKIAELWE TNDEQIFSLR EQHQINRTFK EVDPSAGEFD QHSRTFYSTF
EIENESRPGD SQPILVVGSG PRRLGNGNAN DYVISRVMNE LRNHGYRIVL VNDNPSSPTM
ASLFSDKRYV EPLTNETVMD IVRVENPAKV MVASNQGELL ERLRKHLPES MPLLTIPTAD
QLEDVVSNEP LLEYNALFDG QYVYPLGMTA ALQADDQLNY RTVAKRYPTT LAPADVKKVM
ALGEQSVREL TSPGLYQVLL KTDPLGNYQV QMVRSLPAPD IAFLSKVLQL DLSAVLARLA
INKFSGKLLQ RSMEKQPSQQ RTAVYRALFP FKALQIKEPP TALKVMGAEM QFIE
//
