ID A8SSY7_9FIRM Unreviewed; 1075 AA.
AC A8SSY7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EDP26583.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EDP26583.1};
GN Name=carB {ECO:0000313|EMBL:EDP26583.1};
GN ORFNames=COPEUT_01337 {ECO:0000313|EMBL:EDP26583.1};
OS Coprococcus eutactus ATCC 27759.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Coprococcus.
OX NCBI_TaxID=411474 {ECO:0000313|EMBL:EDP26583.1, ECO:0000313|Proteomes:UP000003518};
RN [1] {ECO:0000313|EMBL:EDP26583.1, ECO:0000313|Proteomes:UP000003518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27759 {ECO:0000313|EMBL:EDP26583.1,
RC ECO:0000313|Proteomes:UP000003518};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Coprococcus_eutactus(ATCC 27759).";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDP26583.1, ECO:0000313|Proteomes:UP000003518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27759 {ECO:0000313|EMBL:EDP26583.1,
RC ECO:0000313|Proteomes:UP000003518};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2007) 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}.
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:EDP26583.1}.
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DR EMBL; ABEY02000014; EDP26583.1; -; Genomic_DNA.
DR RefSeq; WP_004853034.1; NZ_DS483536.1.
DR AlphaFoldDB; A8SSY7; -.
DR STRING; 411474.COPEUT_01337; -.
DR GeneID; 69435025; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_3_9; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000003518; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EDP26583.1};
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 672..863
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 933..1074
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1075 AA; 117770 MW; 436A679F44049A9A CRC64;
MPKREDINKV LIIGSGPIII GQACEFDYSG TQACKALKKL GYEIVLVNSN PATIMTDPET
ADVTYIEPLN VKRLEQIIAK ERPDALLPNL GGQSGLNLCA ELAKEGILDK YNVKVIGVQV
DAIERGEDRI EFKKSMNAIG IEMARSEVAY SVDEALAIAD QLGYPVVLRP AYTMGGAGGG
LVYNKEELKT VCARGLQASL VGQVLVEESI LGWEELELEV VRDCEGNMIT VCFIENIDPL
GVHTGDSFCS APMLTISEDV QKRLQEQAYK IVDSVEVIGG TNVQFAHDPV SDRIIVIEIN
PRTSRSSALA SKATGFPIAL VSAMLATGLT LKDIECGKYG TLDKYVPDGD YVVIKFARWA
FEKFKGVEDK LGTQMRAVGE VMSIGKTYKE AFQKAIRSLE TGRYGLGYTK DYNTKSKDEL
LRMLAHPSSD RHFIMYEALR KGATVDEIFD ITKVKHYFVE QMKELVEEEE ALAAHKGSLP
SDEALTTAKK DGFSDRYLSQ ILEIPEEDIR NKRIELGVTE AWEGVHVSGT KDSAYYYSTY
NAPDSNPINE NKPKVMILGG GPNRIGQGIE FDYCCVHASL ALKKLGFETI IVNCNPETVS
TDYDTSDKLY FEPLTLEDVL SIYNKEKPVG VIAQFGGQTP LNLASDLEKN GVKILGTSPA
VIDLAEDRDL FREMMDKLEI PMPESGMATT VDEALEIAHK IGYPVMVRPS YVLGGRGMEV
VYDDESLDGY MRAAVGVTPD RPILIDRFLN HALECEADAI SDGTHAFVPA VMEHIELAGV
HSGDSACIIP SVHITAENVA TIKEYTKKIA EEMHVVGLMN MQYAIEKGKV YVLEANPRAS
RTVPLVSKVC NVRMVPIATD IITSELTGRP SPVPALKEQH IPYYGVKEAV FPFNMFPEVD
PILGPEMRST GEVLGLSTYY GEAFFKAQEA TQTLLPTSGT VLISVNRKDK DEVIEIAQLF
EKAGFKILAT SGTYAIITAA GVKAEKVKKL QEGRPNINDL ITNGSIDLII NSPSGKESAH
DDSYLRKAAI KAKIPYVTTI AGARATAKGI LYVQAHGDSD VKSLQELHSE IKDAE
//
