ID A0A0L6V0B6_9BASI Unreviewed; 1556 AA.
AC A0A0L6V0B6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Carbamoyl-phosphate synthase small subunit {ECO:0000313|EMBL:KNZ54233.1};
GN ORFNames=VP01_2g1 {ECO:0000313|EMBL:KNZ54233.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ54233.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ54233.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ54233.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KNZ54233.1}.
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DR EMBL; LAVV01007947; KNZ54233.1; -; Genomic_DNA.
DR STRING; 27349.A0A0L6V0B6; -.
DR VEuPathDB; FungiDB:VP01_2g1; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000037035; 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:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 3.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 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; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 3.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
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; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW 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:UP000037035}.
FT DOMAIN 733..929
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1274..1459
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 309..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 473
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 557
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1556 AA; 170880 MW; AFE951B45EA70955 CRC64;
MREKISDPTR LEDIRRLSAV PPNSRSIPSA SDIMSGLDNG LIDGTPLHSP IASVSGIEPL
DVAARRAAAI KGPNGVYIYS SRSSFLSRSP SISGQQRGIH RLPPAAPSVP ALIDLFTASP
GESEDGNSEI CDALAKKVMV LELADGTIYQ GYGFGVSGKS VSGECVFQTG VSPLLAHSAL
ITLSLNPEMK PLLLFFTGMV GYPESLTDPS YKGQILVLTY PLIGSYGVPK REDLMLPTQF
ESSQIHIAAL VIGSYSGDRE DFSHHLADSS LGKWLQEQGV PAIYGVDTRA LTKKIRERGV
MLGKLLSKSV SPPTSSSASS VQKAPLARLS GLGPPRESWR ADYVDVTLHD HNTENLVAIV
SRSKPTLYQP HHLPTCEQPA QILQHPTKSR PLRILALDVG MKYNQVRCFL RRGVEVLAVP
WDHDFLNPSV EKPGSFDALF ISNGPGDPKL AEVPIARIRQ AVEMKAFPIF GICLGHQLLA
LAVGAKTVKL KYGNRGQNIP CTDLQSGRCY ITSQNHGYAV DSASLPDDWK ELFVNANDQS
NEGIYSTRYP YFGVQFHPES APGPQDTKFL FDVFINSVTS FSQDGTFLPV TMPGGTAHEN
SLKNPRVQVK KVLVLGSGGL SIGQAGEFDY SGSQAIKALQ EEGVYTILIN PNIATIQTSK
GLADKVYFLP VTPEFVRKVI QHERPDGIYC TFGGQTALSV GIALADEFEG LGVKVLGTPI
STVVTTEDRE LFASAMAEIG ERCATSASAT SIEASLTAAN QIGYPVIVRA AFALGGLGSG
FANNDEELRE LCDKAFAIST QVLIERSMKG WKEIEYEVVR DCRDNCITVC NMEVSFQNFD
PLGIHTGDSI VVAPSQTLSD ADYQMLRTTA INVIRHLGVV GECNIQYALN PFSKEYAIIE
VNARLSRSSA LASKATGYPL AFIAAKLGLG IPLNEIRNSV TKVTSACFEP SLDYCVVKMP
RWDLKKFQRV SSKLGSSMKS VGEVMAIGRN FEEAIQKAIR SVDPAFTGFD KNSIVSQDQL
KQELSQPTDR RIFAIANAFN EGWSLDEVWE ISRIDKWFLS KLKHLVTMEK IVRRYHASNF
PVNLLRYTKQ LGFSDHQLSR FLNSNELAIR RLRLEFAIMP FVKQIDTVAA EFPAFTNYLF
TSYNATEHDV TFDDRGIIVL GSGVYRIGSS VEFDWCAVRA IRTLRGRGLR TVMVNYNPET
VSTDFDEADR LYFENISLET VLDIYDMEKS SGVIISMGGQ TPNNIALPLH RQNVKIFGTS
PEMIDNAENR YKFSRMLDKI GVDQPRWKEL TTIEEAHLFC ETVGYPVLVR PSYVLSGAAM
NVAYSADDLS AYLAQAAQVS RDRDGRRGSP RKIGHALCLR ARGKRRGDRD GRRGLPRKIG
HALCLRARGK RRETVRRIEI ATEKIGNALN ITGPFNIQFI AKNNDIKVIE CNVRASRSFP
FVSKVTGIDA VAMATDVMMG FPVQPYPTST MPKDYVGIKA PQFSFSRLAG ADPVLGVEMS
STGEVACFGK DKYEAYLKAI LATNVRLPRK SVLFSIGAYA DKLEMLPSVQ RLHRLG
//
