ID W4V8P2_9FIRM Unreviewed; 695 AA.
AC W4V8P2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Carbamoyl-phosphate synthase {ECO:0000313|EMBL:GAE89198.1};
GN ORFNames=JCM21531_2702 {ECO:0000313|EMBL:GAE89198.1};
OS Acetivibrio straminisolvens JCM 21531.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE89198.1, ECO:0000313|Proteomes:UP000019109};
RN [1] {ECO:0000313|EMBL:GAE89198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE89198.1};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Clostridium straminisolvens Strain JCM 21531T,
RT Isolated from a Cellulose-Degrading Bacterial Community.";
RL Genome Announc. 2:e00110-14(2014).
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:GAE89198.1}.
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DR EMBL; BAVR01000032; GAE89198.1; -; Genomic_DNA.
DR AlphaFoldDB; W4V8P2; -.
DR STRING; 1294263.JCM21531_2702; -.
DR Proteomes; UP000019109; 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; -; 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 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; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 2.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
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:UP000019109};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 42..107
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 454..644
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 695 AA; 77649 MW; 9B8F6D45F5E7BAD5 CRC64;
MRDGKGNVIT VCNMENIDPV GVHTGDSIVV APSQTLADRE YQMLRSAALK IISALGIEGG
CNVQFALNPN SFEYAVIEVN PRVSRSSALA SKATGYPIAK VASKIAIGYG LDEIKNAVTG
KTYACFEPTL DYVVLKIPKW PFDKFVKAKR TLGTQMKATG EVMAISSSFE GALMKALRSL
ELGIFTLEQD IYKKFSDEEI REKIKDVNDE RLLVIAEGIR RGITVEEIND ITKIDLFFLN
KIKKLVLMEE KLKTMKLSDF DKENLRTVKK MGFTDAVIAN YIGCGKKEVT AKRKELDIHA
VYKMVDTCAA EFEAMTPYYY STYDECCEVK KSNSKKVLVI GSGPIRIGQG IEFDYCSVHS
VWGLKQEGYE TIIANNNPET VSTDFDTADR LYFEPLTPED VENIVEKEGV EGAIVQFGGQ
TAIKLTKALV EMGVKIFGTE PKYIDAAEDR EKFDEILENL GIPRPKGRTI FTLDEALKAA
NDLGYPVLVR PSYVLGGQGM EIAYSDKDVI EFMEIINRVK QEHPILIDKY MMGKEIEVDA
ICDGEDILIP GIMEHLERAG VHSGDSISVY PTQTIEEKLK EKIVDYTKKL ANALNVVGLI
NIQYVYYNNE LYVIEVNPRS SRTVPYISKV TGIPMVNIAT RIMMGKKLKD FNYGTGLYKE
SEYVAIKVPV FSFEKLHDVD TSLGPEMKST GEVWV
//
