ID U1QMK1_9EURY Unreviewed; 762 AA.
AC U1QMK1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Carbamoylphosphate synthase large subunit {ECO:0000313|EMBL:ERH08253.1};
DE Flags: Fragment;
GN ORFNames=J07HN4v3_00619 {ECO:0000313|EMBL:ERH08253.1};
OS Halonotius sp. J07HN4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halonotius.
OX NCBI_TaxID=1070774 {ECO:0000313|EMBL:ERH08253.1, ECO:0000313|Proteomes:UP000030639};
RN [1] {ECO:0000313|EMBL:ERH08253.1, ECO:0000313|Proteomes:UP000030639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HN4 {ECO:0000313|Proteomes:UP000030639};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
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}.
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DR EMBL; KE356577; ERH08253.1; -; Genomic_DNA.
DR AlphaFoldDB; U1QMK1; -.
DR eggNOG; arCOG01594; Archaea.
DR HOGENOM; CLU_365857_0_0_2; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000030639; 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; -; 1.
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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR016185; PreATP-grasp_dom_sf.
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 PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000030639};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 2..40
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 393..584
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ERH08253.1"
SQ SEQUENCE 762 AA; 82257 MW; 3EEAC655392C86E1 CRC64;
GTPGGEYRVV EVNPRVSRSS ALASKATGYP IARVTAKVAL GKRLHEITNE ITGETTAAFE
PAIDYVVTKV PRWPIDKFDD VDFEIDTAMK STGEAMAIGS TFEESLMKAL RSSEYDPAVN
WHEVDGKTLE AEYLERPSPD RPYAMFEAFD RGYSVQEIID LTGIKEWYVE RFKRIADSAQ
AAQDGDFTPA ATSGYTNNEI AEIADGGVDV DTIEQEVPGR NYKQVDTCAG EFRAETPYYY
SARLPEFHSG PLLGDEAAGE LRVDKETESV VVVGGGPIRI GQGVEFDYCS VHAVQALRDL
DVEAHVVNNN PETVSTDYDT SDGLFFDPIS AEEVADVVEA TGADGVMVQF GGQTSVNIGD
PLKDEIDRRG LDCEIMGTTV EAMDLAEDRD RFNELMGDLG IAQPEGGTAT SENEALELAH
DIGYPVLVRP SYVLGGRAMR VVHDDAELEH YIEEAVRVSP DKPILIDEFL SDAVELDVDA
VADGEDVLIG GIMEHVESAG VHSGDSACMI PPRSLSEETL ARVREVTEDI AAALETVGLL
NVQLAVRDGE VYVLEANPRS SRTVPFVSKA TGVPIAKLAA QVMTGRSLDE IDAAEQIPEQ
TSVKEVVLPF DRLQGSDPRL GPEMKSTGEV MGSADSFGKA YDKAQDATGK PIPKSGTIAL
DLSAEAFPDP DTEAGEALAD GFGEFFEFSE AVDLIDAARA GELDIIVSRD RDLLEVAVEE
EITYFSTPAS ANAALEALQA SDEPIDVKSI ASRPKRADQW GK
//
