ID A0A1G6BNJ5_EUBOX Unreviewed; 1073 AA.
AC A0A1G6BNJ5;
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:SDB22184.1};
GN ORFNames=SAMN02910417_01669 {ECO:0000313|EMBL:SDB22184.1};
OS Eubacterium oxidoreducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1732 {ECO:0000313|EMBL:SDB22184.1, ECO:0000313|Proteomes:UP000199228};
RN [1] {ECO:0000313|EMBL:SDB22184.1, ECO:0000313|Proteomes:UP000199228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3217 {ECO:0000313|EMBL:SDB22184.1,
RC ECO:0000313|Proteomes:UP000199228};
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; FMXR01000011; SDB22184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6BNJ5; -.
DR STRING; 1732.SAMN02910417_01669; -.
DR OrthoDB; 9804197at2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000199228; 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:UP000199228};
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..1073
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1073 AA; 118396 MW; 91C5248D10909C42 CRC64;
MSQRTDIKKI LIIGSGPIVI GQACEFDYSG TQACKALKSL GYEIVLVNSN PATIMTDPEM
ADITYIEPLN VKRLEQIIAK ERPDALLPNL GGQSGLNLCS ELYKEGILDK YAVKVIGVQV
DAIERGEDRI EFKDTMNKLG VEMARSEVAY SVEEALEIAD ELGYPVVLRP AYTMGGAGGG
LVYNKEELKT VCQRGLQASL IGQVLVEESI LGWEELELEV VRDKDNNMIT ICFIENVDPV
GMHTGDSFCT APFLTIDDEL AQELQRQAYK IVEHIGVIGG TNVQFAHDPV SGRVVVIEIN
PRTSRSSALA SKATGFPIAL VSAKLATGLT LAELPCGKYG TLDKYVPDGD YVVVKFARWA
FEKFKGVEDK LGTQMRAVGE VMSIGKNYKE AFQKAIRSLE KDRYGLGFVK NFHEMTKDEL
LKALITPSSE RHFQMYEALR KGATVDEIFE ITKVKKYFIE QMKELVDEEE ELLQHKGDVP
ADEVLIQAKK DGFSDKYLAQ ILEISEDEIR NKRKALGVSE TWDGVHVSGT PDSSYYYSTY
NAPDNNPVNN GKQKIMILGG GPNRIGQGIE FDYCCVHAAQ SLKKLGFETI IVNCNPETVS
TDYDTSDKLY FEPLTLEDVL SIYEKEQPVG VIAQFGGQTP LNLAESLKAN GVKILGTSPE
VIALAEDRDL FRAMMDKLEI PMPEAGMATT VEEALDTAHK IGYPVMVRPS FVLGGRGMEV
VYDDESLRDY MAAAIGVTPD RPILIDRFLN HAMECEADAI SDGTTAYVPA VMEHIELAGI
HSGDSACIIP SKHISEKNLE TIKEYTRKIA EEMHVVGLMN MQYAIENDKV YVIEANPRAS
RTVPLVSKVC GIRMVPLAVD IITSELTGRP SPVKNLGDRK IPYYGVKEAV FPFNMFPEVD
PILGPEMRST GEVLGISKTN GEAYFKAQEG AKAELPLEGV ALISVNKKDK PEAPEVARLL
YETGFKILAT GETCDLIQKE GVPCEKVKKL YEGRPNIMDM ITNGEIDFIV NTPSGKDAVH
DDSYLRKTAI KARVPYITTM TGAKAAAEGI KYVKEQGDDD IMSLQEWHAQ IND
//
