ID D8UHV7_VOLCA Unreviewed; 1176 AA.
AC D8UHV7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFJ40705.1};
GN ORFNames=VOLCADRAFT_77870 {ECO:0000313|EMBL:EFJ40705.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ40705.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; GL378409; EFJ40705.1; -; Genomic_DNA.
DR RefSeq; XP_002958251.1; XM_002958205.1.
DR AlphaFoldDB; D8UHV7; -.
DR STRING; 3068.D8UHV7; -.
DR GeneID; 9623330; -.
DR KEGG; vcn:VOLCADRAFT_77870; -.
DR eggNOG; KOG0370; Eukaryota.
DR InParanoid; D8UHV7; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001058; 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:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01424; MGS_CPS_II; 1.
DR Gene3D; 3.40.50.20; -; 2.
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 HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR InterPro; IPR011761; ATP-grasp.
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; IPR033937; MGS_CPS_CarB.
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; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000001058};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 212..408
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 769..961
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1028..1176
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1176 AA; 127919 MW; CCA9CB34ACE17FA8 CRC64;
MSAQLLSGGA VCGVGRAAPP SSQRNVVFSR PIVVGSHSEL GLKPSSRAAQ RSSRGVKTLR
VSASSTTATP LPWQAAMSEI KKRRDINTIM IIGAGPIVIG QACEFDYSGT QACKSLKKEG
YRVILLNSNP ATIMTDPGMA DRTYVGPMTP ELAEQILAKE RPDAILPTMG GQTGLNLAKT
LAERGILAKY GIELIGAKLP SIDRAEDREL FKQSMTRIGL KCAKSATATT LEEALTIAAD
IGKYPIIVRP AFTLGGTGGG IAYNIDELKE IVTGGLTASM TSQVLVEQSL LGWKEFELEV
MRDLNDNCMI VCSIENVDPM GVHTGDSITV APSQTLTDKE LQRLRDAAIA IIREMGVECG
GSNVQMAVNP EDGEMVIIEM NPRVSRSSAL ASKATGFPIA KMAAKLAVGY TLDQIANDIT
LKTPASFEPS IDYVVTKVPR FAFEKFPGSK AELTTMMKSV GEVMAIGRTW QESLQKALRG
METGLDGWAL PKNYKRLPRD QLMYKLRVPN PDRIVIMFQA MEEGLTDADL FELTKIDPWW
LAQMRELFNV SKWLKSKKLT ELTAEEMAWL KQKGFSDSQI ARYTGSAMMD VRSYRKSLGV
EPSYKRVDTC AAEFEANTPY MYSTYDGNSE CVPTTARKVL ILGGGPNRIG QGIEFDYCCC
HASFSLRKQG YETIMMNCNP ETVSTDYDTS TRLYFEPITV EDVLNVIEAE RPEGVIVQFG
GQTPLKIAMD LDKALKANPI PAASGNGNVC VWGTSPESID IAEDRDRWME LLTKLNIRQP
AGGSARSEEE AFEKASKLGY PVMIRPSYVL GGRAMEILYS NEDLKRYVTF AVEVDPERPV
LIDKYLDRAV ELDVDALCDK DGNVVIAGIM EHIEQAGIHS GDSACSLPTQ TIPPKVLDEI
RSWTISVAKA LNVVGLINIQ FAVQDDVPYI IEANPRASRT VPFVAKAVGH PIAKYASLLM
SGKTLADIGF TEEPIPPHVA VKEVVLPFNK FPGADTLLGP EMRSTGEVMG IDKEFSAAFA
KAQIAAGQRL PKTGKVFISM ADKYKPDIIA VARDLGNLGF GLVATTGTAM ALRAAGVPCE
QVFKIQEGRP NPSDLMKNGE VSLVMMTSSG DEADLRDGKE LRRLALSLSI PTVTTVAGAR
ATTAALRAMR AGPLVQIPLQ DFFPNYYDDS LELMLK
//
