ID A0A1I7G4J9_9FIRM Unreviewed; 1082 AA.
AC A0A1I7G4J9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SFU43397.1};
GN ORFNames=SAMN02910342_00495 {ECO:0000313|EMBL:SFU43397.1};
OS Butyrivibrio sp. INlla21.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520811 {ECO:0000313|EMBL:SFU43397.1, ECO:0000313|Proteomes:UP000198910};
RN [1] {ECO:0000313|EMBL:SFU43397.1, ECO:0000313|Proteomes:UP000198910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INlla21 {ECO:0000313|EMBL:SFU43397.1,
RC ECO:0000313|Proteomes:UP000198910};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; FPCC01000003; SFU43397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7G4J9; -.
DR STRING; 1520811.SAMN02910342_00495; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000198910; 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:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR CDD; cd01424; MGS_CPS_II; 1.
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 Gene3D; 3.40.50.1380; Methylglyoxal synthase-like 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; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR033937; MGS_CPS_CarB.
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 Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
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.
DR PROSITE; PS51855; MGS; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
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 678..869
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 943..1082
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1082 AA; 118394 MW; 46FEAC04FD769FB2 CRC64;
MGQRTDIHKV LIIGSGPIVI GQACEFDYSG TQACKALRSL GYEIVLVNSN PATIMTDPEM
ADKTYIEPLN VDRVAAVIEK ERPDALLPNL GGQSGLNLCS ELYQAGILDK YNVKVIGVQV
DAIERGEDRT EFKKTMDMLG IEMARSKACY SIEEALAEAD ELGYPVVLRP AYTMGGAGGG
LVYNKEELQT VCARGLQASI IHQVLVEESI LGWEELELEV VRDKDNNMIT VCFIENVDPV
GVHTGDSFCT APMLTIDEDL QKELQRQAYK IVEHIGVIGG TNVQFAHDPV SGRIIVIEIN
PRTSRSSALA SKATGFPIAL VSAKLATGLT LAELPDSKFG TLDKYVPNGD YVVVKFARWA
FEKFHGVEDK LGTQMRAVGE VMSIGKNFKE AFQKAIRSLE KDRYGLGAIE KFEKMDKKEL
LRLLKDASSE RYFLMYEAMK KGVTVDELYD ITKVKHYFLN QIKELVDEEV ELVNKYKGTV
PAASDLITAK EDGFADKYLA KVLGVTEDDI REGREKAGLT ESWDGVHVYG TNGSAYYYST
YQNEDNAGAN ETPDTAGSNK IMILGGGPNR IGQGIEFDYC CVHAAMALKK LGFETIIVNC
NPETVSTDYD TSDKLYFEPL TLEDVLQIYR KEKPLGVIAQ FGGQTPLNLA AKLKEEGVNI
LGTTPEVIDL AEDRDQFRMM MDKLGIPMAE SGMASDVEGA KEIAAKIGYP VMVRPSFVLG
GRGMEIVRDE ESMEGYMKAA VGVTPDRPIL IDRFLHNALE CEADAISDGK EAFVPAVMEH
IELAGIHSGD SACIIPSKHI SEKNLRTIEE YTKKIAVEMN VVGLMNMQYA IEDDTVYVLE
ANPRASRTVP LVSKVCGIKM VPVATDIITA SLTGRKSPVE DLIAAKKNTE PAYYGVKEAV
FPFNMFPEVD PVLGPEMRST GEVLGLAKTP GEAFFKAQEA ANAALPTEGA VLISLNNEDK
PNASALAKSF AEDGFKIYAT GKTYDLIKEA GIEVGKVMKN YEGGRPNIED LIKNDEVQLI
INTPIGKDTE HDDGYVRRAA IKARIPYITT VAAAKAAAEG IHEVKTKGCG NINSLQDYHG
QL
//
