ID A0A484G6J5_COLOR Unreviewed; 1635 AA.
AC A0A484G6J5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ammonium-dependent carbamoyl phosphate synthetase {ECO:0000256|ARBA:ARBA00044318};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.3.4.16 {ECO:0000256|ARBA:ARBA00044063};
DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE AltName: Full=Arginine-specific carbamoyl phosphate synthetase, ammonia chain {ECO:0000256|ARBA:ARBA00044249};
DE AltName: Full=Glutamine-dependent carbamoyl phosphate synthetase {ECO:0000256|ARBA:ARBA00044334};
GN Name=arg4 {ECO:0000313|EMBL:TDZ25942.1};
GN ORFNames=Cob_v000929 {ECO:0000313|EMBL:TDZ25942.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ25942.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001777};
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 -!- SUBUNIT: Heterodimer composed of 2 chains; the small (or glutamine)
CC chain promotes the hydrolysis of glutamine to ammonia, which is used by
CC the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000256|ARBA:ARBA00044031}.
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:TDZ25942.1}.
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DR EMBL; AMCV02000001; TDZ25942.1; -; Genomic_DNA.
DR STRING; 1213857.A0A484G6J5; -.
DR Proteomes; UP000014480; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd01423; MGS_CPS_I_III; 1.
DR CDD; cd00496; PheRS_alpha_core; 1.
DR Gene3D; 1.10.10.2320; -; 1.
DR Gene3D; 1.10.10.2330; -; 1.
DR Gene3D; 3.30.1370.240; -; 1.
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 Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR040725; PheRS_DBD3.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR00468; pheS; 1.
DR PANTHER; PTHR11405:SF57; CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF18553; PheRS_DBD3; 1.
DR Pfam; PF01409; tRNA-synt_2d; 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; SSF55681; Class II aaRS and biotin synthetases; 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; PS50862; AA_TRNA_LIGASE_II; 1.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000014480};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 230..511
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 684..876
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1221..1418
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1486..1635
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1635 AA; 180840 MW; 424E28F689146776 CRC64;
MATSSNGPSG DLTSQILLAL SKKDPILSAE HFPEFQFVDI KAALDRLASR SMVTYQSIDR
EEAILEPEGQ QQAEHGSHEA RVFEAVRQAM EGLTIQELES AIGDKNVTKL GQGKAFKNKW
VKKEASGKLV ATADAIKDDT QAQLKQIRDT KTHEPSVITD LKKRKLIKTQ KIITFKIQKG
PEFALEIKKE ETDLTADMIA SGSWKTASFK PYNFKALGAD QNAGALHPLN KVRHEFRQIF
FEMGFEEMDT SKFVESGFWN FDALFVPQQH PARDLQDTFY VSDPKIAGKP GPESKEDNKD
YETYWDNVKE VHQDGKFGSI GYRYPWSADE SLRLVLRTHT TAISTAVLHR LAAKTGPDGR
PPPARYFSID RVFRNESVDA THLAEFHQVE GVIADYGLTL GGLMEFMEIF FNKMGITDIK
FKPAYNPYTE PSMEIFSFHK SLNKIVEIGN SGMFRPEMLE AMGLPKDMTV FGFGLSLERP
CMINCELHVA VMGSYDTAIA QQPKSLSTVV PQVQNNSARL LQKRLFTASA LRPSAQDAPN
PKAYLESGVV KESIGTDVKK VIVIGSGGLA IGQAGEFDYS GAQALKALKE AGVKSVLINP
NIATIQTNHS LADEVYYLPV TPEYVSYVIE KEKPDGIFLS FGGQTALNLG VQMERLGLFE
KYGVKVLGTS VRTLEVSEDR DLFARALEEI NIPIAKSIAV STVEGALDAA NKVGYPIIVR
AAYALGGLGS GFANNEEELR NMAARSLTLS PQILVEKSLK GWKELEYEVV RDANNNCITV
CNMENFDPLG IHTGDSIVVA PSQTLSDEEY HMLRSAAIKI IRHLGVVGEC NVQYALQPDG
LDYRVIEVNA RLSRSSALAS KATGYPLAYT AAKIGLGHTL PLLPNAVTKT TTANFEPSLD
YVVVKVPRWD LAKFQHVKRD IGSAMKSVGE VMAIGRTFEE SFQKALRKVD PKFVGFQGDK
FDDLDFELQN PTDRRWLAVG QAMFHEKYSV DKIHELTKID KWFLYKLQNI VDCTRELEQA
GGLEALKKDL VMKAKKLGFS DLQIAKAVGS NEIEVRKVRL GFGIRPWVKK IDTLAAEFPA
DTNYLYTTYN ASSHDVTFDD KGIIVLGSGV YRIGSSVEFD WCATGATQAL RKMGKKTVVI
NTNPETMSTD YDMADKLYFD ELSYERVMDI YELENSSGVV VSVGGQLPQN IAKDLQEVGG
AVVLGTDPLD IDKAEDRQKF SEILDSIGVD QPAWSELTSV QEAEAFAEQV GYPVLVRPSY
VLSGAAMTVI RSKEDLKEKL EAASSVSPDH PVVITKFIEG AQEIDVDGVA SDGKLIVHAV
SEHVEQAGVH SGDATLVLPP VNLDQTTMER CKEIAQKVAK AWKITGPFNM QIIKADNPEG
GEPALKVIEC NLRASRSFPF VSKVLGVNFI DVATKALVGQ DVPAPQDLMA VKRDYLATKV
PQFSWTRLAG ADPFLGVEMA STGEIACFGK DLVEAYWTSL QSIMNFRMPE PGEGLLFGGE
LKKEWLTSVV DYLQPHGYKL YAADEEVKQF IESTAKGKVS VDVIEFPKED KRALREVFQK
YDIRGVFNLA QARGKTIMDV DYVMRRNAVD FGVPLFMEPK TAVLFAQCMS EKLPRKEGIP
SEVRPWSNFL GGKPL
//
