ID I0API1_IGNAJ Unreviewed; 1066 AA.
AC I0API1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Carbamoylphosphate synthase large subunit {ECO:0000313|EMBL:AFH50888.1};
GN Name=carB {ECO:0000313|EMBL:AFH50888.1};
GN OrderedLocusNames=IALB_3185 {ECO:0000313|EMBL:AFH50888.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH50888.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH50888.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH50888.1; -; Genomic_DNA.
DR RefSeq; WP_014562022.1; NC_017464.1.
DR AlphaFoldDB; I0API1; -.
DR STRING; 945713.IALB_3185; -.
DR GeneID; 78244697; -.
DR KEGG; ial:IALB_3185; -.
DR PATRIC; fig|945713.3.peg.3212; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_3_10; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000007394; Chromosome.
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:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01423; MGS_CPS_I_III; 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; 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; 2.
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:UP000007394};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 671..862
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 928..1066
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1066 AA; 119152 MW; D2ED0D0C4E44BFBD CRC64;
MIKKGKPKKV LILGSGALQI GQAGEFDYSG SQAIKALRED AVETILINPN IATIQTSENF
ADKVYFIPIK ADFVERVIEK EKPDGILLQF GGQTALNVGV ELYDKGILAK YNVKVLGTPV
ETIKDTEDRL LFAKRVEEIG LKVAKSKTAT NLDEAIQAGK QIGYPLMVRI AYALGGLGSG
IVNNEKELIE KARRAFSFTN QILIEESLYG WKEVEYEIVR DKYNNCITVC SMENIDPMGI
HTGDSVVIAP VQTLSARENF KLRSIGIKLI RHLGIIGECN IQYALDPNSE DYRIIEVNAR
LSRSSALASK ATGYPLAFIA TKLALGYALN EVVNAITQET SANFEPALDY VALKFPRWDL
QKFQQVSTQL GSEMKSVGEV MSLGRSFEEV LQKAIRMLDV GMKGFVGNEL HFENLDKELS
EPTDKRIFAI AEALRKGYSV DRIHELTKIT KWFLYKMKNI VDIETKLRGF KNLESLDAEL
MKAAKQSGFS DLQIAQLVNS DEMSVRKFRK SIGVVPVIKQ IDTMAAEFPA QTNYLYLTYH
GEEDDIKSGE KDHIIVLGSG PYRIGSSVEF DWCCVNAATQ VNKSGYKSIM INCNPETVST
DYDICDKLYF EQLTLERVLD ICDKENPAGV IVSMGGQTPN NLAMKLHKVG IKIIGTTPEQ
IDNAESRHKF SQILDEIEVD QPEWREVTTL EDAKQFSKNV GYPVLIRPSY VLSGAAMSIV
LTEDELELYL KKATELNTEH PIVISKFITD AREIEVDAVA TEGELFCYAI AEHVENAGVH
SGDATIVLPP QRTYLETMRR VKLITKKIAK ALEITGPFNI QFIAKDNEVK VIECNLRASR
SFPFVSKTLK INFIEIATRL MLGEKVPRID KSSFDLDYVG VKASQFSFTR LKGSDPVTGV
EMSSTGEVAC LGDDFNEAFL KSVLATGYKI PQKAVLLSTG TPRNKAELID ELLILKKMGL
KFYGTKGTAD FYKHNGGIDV EVLYRPYDNQ EPSILTYMSE GKIDLVINIP KTAEKVELDS
DYIIRRKAVD LNIPLLTNVQ IAKRFIKALE QYNQQELPVK SWDEYV
//
