ID A0A0K8Q5A0_9MICC Unreviewed; 758 AA.
AC A0A0K8Q5A0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:GAP55352.1};
DE Flags: Fragment;
GN ORFNames=AHiyo6_19170 {ECO:0000313|EMBL:GAP55352.1};
OS Arthrobacter sp. Hiyo6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1588022 {ECO:0000313|EMBL:GAP55352.1, ECO:0000313|Proteomes:UP000037466};
RN [1] {ECO:0000313|Proteomes:UP000037466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hiyo6 {ECO:0000313|Proteomes:UP000037466};
RA Hiraoka S., Machiyama A., Iwasaki W.;
RT "Microbial genome analysis of tsunami-affected soil.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAP55352.1, ECO:0000313|Proteomes:UP000037466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hiyo6 {ECO:0000313|EMBL:GAP55352.1,
RC ECO:0000313|Proteomes:UP000037466};
RX PubMed=26764021; DOI=10.1186/s12864-016-2380-4;
RA Hiraoka S., Machiyama A., Ijichi M., Inoue K., Oshima K., Hattori M.,
RA Yoshizawa S., Kogure K., Iwasaki W.;
RT "Genomic and metagenomic analysis of microbes in a soil environment
RT affected by the 2011 Great East Japan Earthquake tsunami.";
RL BMC Genomics 17:53-53(2016).
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:GAP55352.1}.
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DR EMBL; BBUE01000199; GAP55352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K8Q5A0; -.
DR Proteomes; UP000037466; 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 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 Gene3D; 3.40.50.1380; Methylglyoxal synthase-like 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; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
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; 1.
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; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 323..514
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 597..758
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 703..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 758
FT /evidence="ECO:0000313|EMBL:GAP55352.1"
SQ SEQUENCE 758 AA; 82202 MW; D5568C2D47F7CE18 CRC64;
MVKVPRFAFE KFPAADPTLT TTMKSVGEAM AMGRNFTEAL QKALRSLEQK GSQLDFSHVP
EWEVPELIEK SKRPTTERLH QVQRALLGGA SVEQLFEATK IDPWYLDQLQ LLNEISVEIR
KSTALTQEML QRAKRHGFSD EQIGALTHNS EAVVRGVRQA LGIRPVYKTV DTCAAEFAAY
TPYHYSSYDE EDEVALHAKP SIIILGSGPN RIGQGIEFDY SCVHASMALR KAGYETVMVN
CNPETVSTDY DVSTRLYFEP LTLEDVLEVI AAEERTGGVM GVFVQLGGQT PLKLAQQLAD
AGVPILGTSP EAIDLAEHRG AFSRVLDEAG LISPKNGTAV SFEDAKKIAD EIGYPVLVRP
SYVLGGRGME IVYDEPNLSR YIANATEITP DHPVLIDRFL EDAVEIDVDA LYDGTDMYLG
GIMEHIEEAG IHSGDSACVL PPITLGNNVL ERVRTATRAI AEGVGVRGLI NIQFALASDV
LYVLEANPRA SRTVPFVSKA TGVQMAKAAA LIGTGVTINQ LRSAYKMLPE TGDGSTLPLD
APVSVKEAVL PFSRFRTPEG KVVDSLLGPE MRSTGEVMGI DKHFDTAFAK SQAAANNALP
TEGKVFVSVA NRDKRSVIMG VKRLSDLGFE IVSTGGTADV LRRNGIQATP VRKVAEGSSA
EGEGTIADLI IAGEIDMVFN TPSGGEARSD GYELRAAARR LASRASQRWP SSRRRPGHRG
AAHVRVVRHE PAGARRQPRC IPEKSRAECL RSSPVAAR
//
