ID A0A1M4XR42_9CLOT Unreviewed; 1070 AA.
AC A0A1M4XR42;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SHE95712.1};
GN ORFNames=SAMN02745158_02077 {ECO:0000313|EMBL:SHE95712.1};
OS Lactonifactor longoviformis DSM 17459.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Lactonifactor.
OX NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHE95712.1, ECO:0000313|Proteomes:UP000184245};
RN [1] {ECO:0000313|EMBL:SHE95712.1, ECO:0000313|Proteomes:UP000184245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17459 {ECO:0000313|EMBL:SHE95712.1,
RC ECO:0000313|Proteomes:UP000184245};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQVI01000009; SHE95712.1; -; Genomic_DNA.
DR RefSeq; WP_072851368.1; NZ_FQVI01000009.1.
DR AlphaFoldDB; A0A1M4XR42; -.
DR STRING; 1122155.SAMN02745158_02077; -.
DR OrthoDB; 9804197at2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000184245; 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 Reference proteome {ECO:0000313|Proteomes:UP000184245};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 132..326
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 671..862
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 932..1070
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1070 AA; 117273 MW; E89ECBA52417A35C CRC64;
MKREDIHKVL IIGSGPIIIG QACEFDYSGT QACKALKNLG YEIVLVNSNP ATIMTDPETA
DVTYIEPLNV KRLTQIIEKE RPDALLPNLG GQSGLNLCSE LAAAGVLEKY NVKVIGVQVD
AIERGEDRIE FKKTMAGLGI EMARSEVAYS VEEALSIAEK LGYPVVLRPA YTMGGAGGGL
VYNVEELKTV CARGLQASMV GQVLVEESIL GWEELELEVV RDAKNNMITV CFIENIDPLG
VHTGDSFCSA PMLTISQEVQ DRLQEQAYKI VEAIEVIGGT NVQFAHDPVS DRIIVIEINP
RTSRSSALAS KATGFPIALV SAMLASGLTL DEIPCGKYGT LDRYVPGGDY IVIKFARWAF
EKFKGAEDKL GTQMRAVGEV MSIGKTYKEA FQKAIRSLEI GRAGLGGARD FAAKSKKELL
KMLATPSSER HFIMYEALRK GATVEEIFEL TQVKRYFIDQ MKELVEEEEA LKAEKGRIPA
NDVLRQAKLD GFSDKYLGQI LEIPEEQIRT ARTEAGIVEA WEGVHVSGTK DAAYYYSSYH
IKDESPVNTD RPKIMILGGG PNRIGQGIEF DYCCVHAAIA LKELGFETII VNCNPETVST
DYDTSDKLYF EPLTLEDVLS IHEKEKPVGV IAQFGGQTPL NLAEDLKKAG VNILGTTPET
INMAEDRDLF RAMMDKLNIP MPEAGMAVDV EEALAIAEKI GYPVMVRPSF VLGGRGMEVV
HDAEALTYYM KAAVGVTPDR PILIDRFLHH ATECEADAIS DGTDVFVPAV MEHIELAGIH
SGDSACILPS KNLTPEQVAT IKEYTRKIAV EMNVVGLMNM QYAIEDGVVY VLEANPRASR
TVPLVSKVCN IKMVKLATDI MTSHLTGRKS PVPELKEKTF SHYGVKEAVF PFNMFQEVDP
LLGPEMRSTG EVLGMAENFG EAFFKAQEAT KTELPLEGTV LISVSDRDKP EVAEVARGLH
ELGFRLMATG RTQELIADAG IPVKKIAKIN EGRPNILDEM TNQKISMVVN TPVGKKGAVD
DSYIRKAAIK YKIPYVTTMA EAKATVEGIR AAKAGKFSVQ SLQEFHKNIR
//
