ID T1PFQ2_MUSDO Unreviewed; 696 AA.
AC T1PFQ2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE SubName: Full=Carbamoyl-phosphate synthase {ECO:0000313|EMBL:AFP62210.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EMBL:AFP62210.1};
RN [1] {ECO:0000313|EMBL:AFP62210.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ALHF {ECO:0000313|EMBL:AFP62210.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:AFP62210.1};
RA Liu N., Zhang L., Li M., Reid W.;
RT "Transcriptome of adult Musca domestica launches a platform for comparative
RT house fly gene expression and characterization of differential gene
RT expression among resistant and susceptible house flies.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KA647581; AFP62210.1; -; mRNA.
DR AlphaFoldDB; T1PFQ2; -.
DR VEuPathDB; VectorBase:MDOA013020; -.
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 CDD; cd00298; ACD_sHsps_p23-like; 1.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
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; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 25..472
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 144..342
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 615..691
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 696 AA; 77052 MW; 1E50CAA59099FF9C CRC64;
MYTQLIRNLR NIRCYSAKAT PAVRPINKIL IANRGEIACR VIKTARKLGV RTVAVYSDPD
EKSLHTQYAD EAYRVGEAAS ASSYLRGDRI IEIAKTSGCQ AIHPGYGFLS ESVEFAELCQ
KEGVVFMGPP SSAIRDMGIK STSKHIMDAA GVPIINGYHG EDQSDKRLQK EAQKIGFPLM
IKAVRGGGGK GMRIADKQED FMDALNSART ESQKSFGDSS MLLERYVRSP RHVEVQVFAD
QYGNAVYLWE RDCSVQRRHQ KIIEEAPAPG LSEELRRELG EAAVRAAKAV GYVGAGTVEF
IMDKEDLSFH FMEMNTRLQV EHPISEMITG TDLVEWQIRI AAGEPLPVTQ EQITRKGHAF
EARIYAENPR GGFLPGAGPL RYLATPQASD LVRVETGVRE GDEVSVHYDP MIAKLVVWGE
NRSQALNSLI ARLREYHITG LETNINFLID LASHPEFQSG NVHTGFIDQH FDTLFPPVEI
SDNDLCKAAL SLVFNELEAS QTNAPSRHDP FAASANLRLN YDLIRQYQLK ANEKTYQINV
KFNAKNIEIQ IDNGSWYTVK ADRIEDGERL KIRSNIANNI STYNAYIDES EVSVFLENGK
LTFELEQPKF LNAAVDQMGS AGSKVIAPMP GVLEKVLVKS GDKVKKGDNL AVLIAMKMEH
ILKAPKDAVV KSIGGAEGSN VAKGAAVITF EEEAEN
//
