ID A0A0P7WB81_9BACT Unreviewed; 942 AA.
AC A0A0P7WB81;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit CarB {ECO:0000313|EMBL:KPP97058.1};
GN Name=carB {ECO:0000313|EMBL:KPP97058.1};
GN ORFNames=HLUCCA01_12230 {ECO:0000313|EMBL:KPP97058.1};
OS Bacteroidetes bacterium HLUCCA01.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1666909 {ECO:0000313|EMBL:KPP97058.1, ECO:0000313|Proteomes:UP000050310};
RN [1] {ECO:0000313|EMBL:KPP97058.1, ECO:0000313|Proteomes:UP000050310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA01 {ECO:0000313|EMBL:KPP97058.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (AUG-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:KPP97058.1}.
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DR EMBL; LIHN01000015; KPP97058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7WB81; -.
DR STRING; 1666909.HLUCCA01_12230; -.
DR PATRIC; fig|1666909.3.peg.2851; -.
DR Proteomes; UP000050310; 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:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
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; 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; 2.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 681..872
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 942 AA; 105520 MW; 1E6ECBF12094F848 CRC64;
MPRRNDINTI LIIGSGPIII GQACEFDYSG TQACKSLKEE GYRVVLINSN PATIMTDPMM
ADAVYLKPLT TRSIKEICAI ENVDAVLPTM GGQTALNLAR DLHHAGFWEK NNIKIIGVDI
DAIDITEDRQ QFRDLMERID VGQCRSFVAK SLLDAKEIVL KLGGFPLIIR PSFTMGGMGG
GIIWNEEQFE RKVLRGLELS PIHEILLEES IIGWKEFELE LLRDDHDNVV IICGIENFDP
MGVHTGDSVT VAPAQTLTDK QFQLLRDAAI RMMRSIGTFA GGCNVQFAME PGTDRLVAIE
INPRVSRSSA LASKATGYPI AKVASKLAVG YTLDELKNQI TGTTSACFEP AIDYVVVKVP
RFNFEKFPGV DEELGTQMKA VGEVMAIGRN FAEALNKAWQ GMEIGRAGLG ADGYEVLDRK
HVRERLLKPY WDRSLQIRNA FKLGASIEEI HDVTYVDPWF LQQIRYMVSI ENRLEGQTLE
SLGRDELFEA KQAGFSDKQI AWLLSQSATP VTEDQVREKR KSMGMLPSFK LVDTCAAEFP
AQTPYYYSAY EGENESEISD RKKIMILGSG PNRIGQGIEF DYSCTHAVLA AKEMGYETIM
VNCNPETVST DFDVADKLYF EPVFWERVLD IFEHEKPEGV ILQVGGQTAL KLAKHFQRSG
IRIFGTSYDM MDLAEDRGKF SELLVQCDIP FPRYGIASDV ASALEQAEIV GYPVLIRPSY
VLGGQGMRIA VKPEELTEYV EDLLKTHPEN VFLIDHYLDH AIEVDFDSIH DGETLHVSGI
MQHIEPAGVH SGDSTAVLPP YSLSDEVIAT MKDYQNRIAK AMHVVGFINV QYAIKDEVVY
VLEANPRATR TIPFIAKATG RPESAIGVKV MLGARLSEFD LSSKLKHYAI KEPVFPFDKF
PEVKKELGPE MKSTGETIYF MEDFEDEHFR KPYEFKNLYL SR
//
