ID A8ACC3_IGNH4 Unreviewed; 1047 AA.
AC A8ACC3;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:ABU82575.1};
GN OrderedLocusNames=Igni_1399 {ECO:0000313|EMBL:ABU82575.1};
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591 {ECO:0000313|EMBL:ABU82575.1, ECO:0000313|Proteomes:UP000000262};
RN [1] {ECO:0000313|EMBL:ABU82575.1, ECO:0000313|Proteomes:UP000000262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125
RC {ECO:0000313|Proteomes:UP000000262};
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H.Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(2008).
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; CP000816; ABU82575.1; -; Genomic_DNA.
DR RefSeq; WP_012123539.1; NC_009776.1.
DR AlphaFoldDB; A8ACC3; -.
DR STRING; 453591.Igni_1399; -.
DR GeneID; 5561864; -.
DR KEGG; iho:Igni_1399; -.
DR eggNOG; arCOG01594; Archaea.
DR HOGENOM; CLU_000513_1_3_2; -.
DR OrthoDB; 85487at2157; -.
DR PhylomeDB; A8ACC3; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000000262; Chromosome.
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; 3.30.1490.20; 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; 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; 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000000262};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 130..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 657..846
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 914..1047
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1047 AA; 116659 MW; 4208508FD100D4DF CRC64;
MNDLRSVLII GSGAIKIGEA AEFDYSTSQA LKALREEGIE TILVNPNVAT VQTTKEMSDK
LYFVPLRRDI LEKIIEAERP DGILIGFGGQ TALTLGVELW ESGVLQKYGV KVIGTPIEGI
KKATDKTLFA KTMKENGIPM PPSEAASNVD EALEIAERLG YPVIVRIAFT LGGKGSFIAW
NRRELEKWVV RAFAQSAVGR VLVEKYLHHW KEIEFEVVRD AYNNSVAVAC LENLDPMGVH
TGDSVVIAPC QTLTNREYQI LRDASIRVAE VIGLVGEGNV QLALDPRGET YYVIETNPRM
SRSSALASKA TGYPLAYVAA KLALGYKLWE ILNKVTGATC ACFEPSLDYV VIKVPRWDLD
KFEGVEKSLD SEMKSVGEVM AIGRNVAEAL QKAFRMLDIG VEGITDFEPI KVKSKEEALE
KLRKREPYWP LYAAKAIYEG ATLDEVHEAY GVDKYFLHWI KEVVEQKKEI ERSAADYEYS
KILGFSDKEL KVDIRTGLLP KVKRIDTLAA EWPAVTNYLY LTYDGTEDDV KFTDKRYKTM
VLGAGVFKIG ISVEFDWAVV SLVRSLRKYG AEEVITLNYN PETVSTDWDE SDKLYFEEIT
EETVYKVVEK ERPWGVIAFA GGQIANKIYK KIEALGVPLL GTPGRSVDTA EDRKKFSDLL
DKLNIKQPRW VSASSMEELK KFVDEVGFPV IVRPSYVLSG SAMKVVWSWE ELVEFVRKAS
EVSREHPVVV SEFFVGAREA EVDAVSDSAS VVAVPLSHVE PAGVHSGDST MVTPARLEDE
VVNKMLDISL TLARELEIRG PFNIQFLVKN NDPYVIELNL RASRSMPFSS KSRNVNLMEL
SAKVVVEGTL GLGEGVYVPP TKVWGVKSPQ FSWTQLKGAY PDLGPEMRST GEVAAFSRSY
EDALILSWLS AVPNDIPNKD KKVLVYSLEV FDEDRTKAKE AADAMSELGY HVITLEGVEV
KGYEPYDSSK IKEMLVKREI GLVITSGSNR SVDYVVRRTA VDMNVPLVLN SYLGAELSKA
FIKVYEKYGA LDPARLEIKE YGELLGS
//
