ID V5F996_BYSSN Unreviewed; 1781 AA.
AC V5F996;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Ammonium-dependent carbamoyl phosphate synthetase {ECO:0000256|ARBA:ARBA00044318};
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 ORFNames=PVAR5_1257 {ECO:0000313|EMBL:GAD92664.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92664.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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:GAD92664.1}.
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DR EMBL; BAUL01000035; GAD92664.1; -; Genomic_DNA.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_238577_0_0_1; -.
DR InParanoid; V5F996; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000018001; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd01423; MGS_CPS_I_III; 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; 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; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 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 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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000018001};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 831..1023
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1368..1565
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1633..1781
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 171..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 210..237
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 503..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1781 AA; 197065 MW; AB811CCD53737D30 CRC64;
MADHPDTSIS IPPFAKPLAP YLKSRQEAFR IRQILTLYLQ SQLKFTEDGS NAGNQQSQPH
LSLCNPQSVV SVDRVPVDFS GLRKEYLEAL RENVAARREY SALAHDVTSR KLMKTSVAAD
APPSNEPSAE LQTYLSLLRD RRRLEKLRVF EDHLSRLDAP DTSDLDRLYK SGQSPLGTQQ
LDGQIESGSS DSRAMREGLG QLVYKLEKAV LRAKSQLDRE KKLLEDLQAN RESLEEQSTS
GVKVAALQRI RDELVQWVEA KLVASGGEGN DYLPQFSQDE VDDMSKAIEE RKEQIKEQYA
SYVEARRALL DSISVASQPL ASPPAKSPLK STPEGRATGE VLDMEVLDLL PYASEVLLPL
SKTQKSLALQ KTYLSGILAK EKSTARRMLD RLSDESHLLP EYPLLARQPR YKQAVAAISS
RSTVESPEQG KPDEILSRAQ AWAFASDAAR THERAYVEEK TDVGKEMAES AEQTLKEVYE
IINQDYEEEH EAGASQDEGD IWASEIRPTR TRARQGRTEK RTTGRGPWSG LNGPAAKLKS
SSPPRFLSAP ENFLIIIIKL EEQRKQQALA EETLHSVDRG RCGCFCRNSA QTVSNRVPKP
SPLLQIMALP ARCARVSSSL LRQRCLAETR PATLALRSYS TQTAARSTAS ALRLQQKLPS
SYRPQQLRAF SSSLRRLASE AENPPSSKAY FASGVLKDSD NLVDVKKVLV IGSGGLSIGQ
AGEFDYSGSQ ALKALKEAGV QSILVNPNIA TIQTDHKLAD EVYYLPVTPE YVTYVIERER
PDGILLTFGG QTGLNLGVQM NRMGIFDRYG VKVLGTSIKT LETSEDRDLF SKALNEINIP
IAESIAVSTV DEALKAAESI GYPIIVRSAY ALGGLGSGFA NNPEELRNLS SRSLSLAPQI
LVEKSLKGWK EVEYEVVRDA ANNCITVCNM ENFDPLGIHT GDSIVVAPSQ TLSDEEYHML
RTAAIKIVRH LGVVGECNVQ YALQPDGLDY RVIEVNARLS RSSALASKAT GYPLAYTAAK
IGLGHTLPEL PNAVTKTTTA NFEPSLDYIV TKIPRWDLSK FQHVNRDIGS AMKSVGEVMA
IGRTFEESFQ KAIRQVDPRF IGFQGDKFEN LDEVLANPTD RRWLAVGQAM LHENYSVDRV
HELTKIDKWF LYKLQNIVDC QNELKEIGSL FGIKEETMLK AKKLGFSDKQ IALCVGSTED
DVRARRKSFG IRPWVKKIDT LAAEFPADTN YLYTTYNATS HDVTFDDHGT IILGSGVYRI
GSSVEFDWCA VNATLSLRNM GKKTVMINYN PETYSTDFDT ADKLYFEELS YERVMDIYEL
EAATGVVVSV GGQLPQNIAL RLQETGGAKI LGTDPQDIDK AEDRHKFSQI LDSIGVDQPA
WKELTSVAEA EKFAESVGYP VLVRPSYVLS GAAMNVIYSQ GELKEKLLNA SAVSPDHPVV
ITKFIEGAQE IDVDAVGSNG KLILHAISEH VEPAGVHSGD ATLVLPPANL DEKTMARVKE
IAEKVAKAWN ITGPFNMQII KADNEETGES DLKVIECNLR ASRSFPFVSK VLGTNFVDVA
TKALVGRDVP EPVDLMATKR DYLATKVPQF SWTRLAGADP FLGVEMSSTG EIACFGKDLV
EAYWSSLQAT MNFRVPEPGE GLLFGGDLRS YLTQIVEYVQ PLGYKLYAAS PEVKAHLESA
SKGSVSVDVI EFPKQDKRAL REVFQKYDIR GVFNLAKQRG KTLLDEDYVM RRNAVDFGVP
LFMEPKTALL FAQCMNEKLP RKEGIPSEVR SWSDFVGGKL L
//
