ID A0A0M0BTI5_9ARCH Unreviewed; 1067 AA.
AC A0A0M0BTI5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KON31471.1};
GN ORFNames=AC482_00690 {ECO:0000313|EMBL:KON31471.1};
OS miscellaneous Crenarchaeota group-15 archaeon DG-45.
OC Archaea; Candidatus Bathyarchaeota; MCG-15.
OX NCBI_TaxID=1685127 {ECO:0000313|EMBL:KON31471.1, ECO:0000313|Proteomes:UP000037210};
RN [1] {ECO:0000313|EMBL:KON31471.1, ECO:0000313|Proteomes:UP000037210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG-45 {ECO:0000313|EMBL:KON31471.1};
RA Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA Teske A.P.;
RT "New insights into the roles of widespread benthic archaea in carbon and
RT nitrogen cycling.";
RL Submitted (JUN-2015) 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 -!- 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:KON31471.1}.
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DR EMBL; LFWZ01000004; KON31471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0BTI5; -.
DR PATRIC; fig|1685127.3.peg.57; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000037210; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 2.
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; 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; 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; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
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 926..1067
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1067 AA; 115336 MW; 537586A1FBA5CE32 CRC64;
MPRLEGVEKV VVLGSGAIKI GEAGEFDYSG AQAVKALREE GISVVLVNPN IATIQTDAKL
ADRVHFLPVT AEHVEGVIED ERPDGILLGF GGQTALNCGV DLAERGVLDR WGAAVLGTGI
RAIEVCDDRD QFRGLMIENG VPIPRSGSAS TVERAVEVAR EIGYPIMVRV AYTLGGQGTG
VAHDEEGLRE IASRGLAHSR IGQVLVEEYL GKWKEIEYEV MRDAADNCVI VCNMENLDPM
GVHTGDSIVV APSQTLTNGE YHRLRIIAFK VVRALGIVGE CNIQFALDPG SDGVRVIEVN
SRLSRSSALA SKATGYPIAY IAAKLAVGYT LPELVNKVTG VTTACFEPAL DYVVVKVPRW
DFQKFRNVDR GIGTQMRSVG EVMAVGRTFK EAIQKAVRMS EMGRELTDPD GAEGDPGTLM
RSLEHPTDRR LFHIMEALET GVPIGDIGGM TGIDPWFLHE LKEIVDFKEI LAAEPLAPGL
LREAKRLGFS DRVIGRLAGR TEDEVRALRA ALGIRPVVKQ IDTLAAEWPA TTNYLYMTYN
GDEDDVEFEA GRGAVVLGSG CYRIGSSVEF DWCCVNMAWA LKGEGVGEVV MVNCNPETVS
TDFDVLDKLY FEELTYERVM DIVERESPLG VVVSVGGQTP NNLALRLAGR GVSILGTEAA
SVDVAEDRAK FSRLLDELRV RQPAWRRVES IGGAKAFAAE VGYPVLVRPS YILSGSAMSV
ALDEGELEVY LGKAARVSRG YPVVVSKFIV DAKEVDVDAV SDGRNVFIGA IIEHIEKAGV
HSGDATMVVP TLTLDGEVED QIRRCTRMIA RGLGIRGPFN IQYLVRDDEI YVIECNLRAS
RSMPYVSKSV GVNLMELAAV ALLGGEVPDG EGVPDRYCVK APQFSFMRLD GADPVTGVEM
VSTGEVACFG ERFEEALVKA LAASGMKLPG EGDPIMISVG GEKGKAVEIA RKIAAKGFKI
YATEHTAEAL RVSGIDYEVI HKVSDGVRPN ALDFIEARNL KLIINSPSPD RMEPRAVTDG
YLIRRKAVEF GIPIITNLEL ADALAEALMN HEGKQVITAA AVAPPPL
//
