ID M7Y472_9BACT Unreviewed; 939 AA.
AC M7Y472;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:EMS32056.1};
GN ORFNames=C943_01621 {ECO:0000313|EMBL:EMS32056.1};
OS Mariniradius saccharolyticus AK6.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Mariniradius.
OX NCBI_TaxID=1239962 {ECO:0000313|EMBL:EMS32056.1, ECO:0000313|Proteomes:UP000010953};
RN [1] {ECO:0000313|EMBL:EMS32056.1, ECO:0000313|Proteomes:UP000010953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK6 {ECO:0000313|EMBL:EMS32056.1,
RC ECO:0000313|Proteomes:UP000010953};
RA Vaidya B., Khatri I., Tanuku N.R.S., Subramanian S., Pinnaka A.;
RT "Genome assembly of Mariniradius saccharolyticus AK6.";
RL Submitted (JAN-2013) 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:EMS32056.1}.
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DR EMBL; AMZY02000015; EMS32056.1; -; Genomic_DNA.
DR RefSeq; WP_008629669.1; NZ_AMZY02000015.1.
DR AlphaFoldDB; M7Y472; -.
DR STRING; 1239962.C943_01621; -.
DR eggNOG; COG0458; Bacteria.
DR InParanoid; M7Y472; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000010953; 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 SMART; SM01209; GARS_A; 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 Reference proteome {ECO:0000313|Proteomes:UP000010953};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 134..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 677..868
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 939 AA; 104918 MW; 3DE7F4387D002085 CRC64;
MPKDSSIKHV LIIGSGPIVI GQACEFDYSG SQAARSLREE GIKVTLINSN PATIMTDPVT
ADHVYLQPLE KKSIVKILNE HPDIDAVLPT MGGQTALNLA IDCEKAGIWK KFGVRMIGVD
IDAIDTAENR EKFKALMEKI GVDVCKGDTA TSFLHGKEIA QEIGFPLIIR ASYTLGGAGG
AFVEKAEDFE KALMAGLQAS PVHEVLIEQS ILGWKEYELE VMRDNIGNMI VVCSIENFDP
MGIHTGDSIT VAPAMTLPDT VYQRMRNHAI TMMNSIGNFA GGCNVQFAVS PDNQTIIGIE
INPRVSRSSA LASKATGYPI AKVAAKLAIG YNLDELKNSI TGNTSAFFEP AIDYVIVKIP
RWNFDKFKGS DRRLGLSMKA VGEVMGIGRN FQEALQKACQ SLEIKRNGLG ADGRELKDQA
RLLHSLANPS WDRLFHVYDA FKLGISFRTI HDLTKIDKWF LRQIEELVHI EAEIEKHTLD
SIPKELVDRA KKKGYADRQL AHMLGCLESE IFNKRYHDMG IRRVYKLVDT CAAEFEAQTP
YYYSTFGEEN ESKTSDRKKV VVLGSGPNRV GQGIEFDYSC VHGVLAAKEC GYETIMINCN
PETVSTDFDI SDKLYFEPVF WEHIYEIILQ ENPIGVIVQL GGQTALKLAE KLHKYGIKII
GTSFDALDLA EDRGRFSTLL KENDVPYPEF GTIHNTDEAL ELCKRIGFPL LVRPSYVLGG
QGMKIVINEQ ELEEHVVNVL RDIPNNEILL DHFLEGAIEA EADAICDGEN VYIIGIMQHI
EPAGIHSGDS YAVLPPYNLG DYVMRQIETY TKKIALALRT VGLINIQFAI KNDRVYVIEA
NPRASRTVPF ICKAYQEPYV NYAVKVMLGE KKVTDFDFKP VKNGYAIKEP VFSFHKFPNV
NKELGPEMKS TGEAIYFIED LMDDYFMKIY SERNLYLSR
//
