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Database: UniProt
Entry: A0A1F4JHU5_9BURK
LinkDB: A0A1F4JHU5_9BURK
Original site: A0A1F4JHU5_9BURK 
ID   A0A1F4JHU5_9BURK        Unreviewed;      1102 AA.
AC   A0A1F4JHU5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:OGB22040.1};
GN   ORFNames=A3I66_19265 {ECO:0000313|EMBL:OGB22040.1};
OS   Burkholderiales bacterium RIFCSPLOWO2_02_FULL_57_36.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=1797562 {ECO:0000313|EMBL:OGB22040.1, ECO:0000313|Proteomes:UP000176765};
RN   [1] {ECO:0000313|EMBL:OGB22040.1, ECO:0000313|Proteomes:UP000176765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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:OGB22040.1}.
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DR   EMBL; MESE01000115; OGB22040.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4JHU5; -.
DR   STRING; 1797562.A3I66_19265; -.
DR   Proteomes; UP000176765; 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:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 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; IPR034733; AcCoA_carboxyl_beta.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR48095:SF5; BLL7292 PROTEIN; 1.
DR   PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
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; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT   DOMAIN          2..460
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..323
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          487..565
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          849..1084
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          476..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1102 AA;  118397 MW;  F553F76926FD3CF2 CRC64;
     MTITTLLIAN RGEIAIRIAR AAAELNIRTV AIYSKDDAAS LHVRKTDEAY ALPGSGAAAY
     LDIEQILTAA RKAKCGAIHP GYGFLSENAQ FARRCAEEGI VFVGPSPEIL SLFGDKVQAR
     KLAERNHVPV VPGTAGSTSL DQAHQFFTSL GQGGAMMIKA IAGGGGRGMR AVHRSDEIDS
     AFARCRSEAL AAFGNGDLYV EQLVQFARHI EVQIIGDGTG RISHLGEREC TLQRRQQKLV
     EIAPSPSLSA AMRTRLTAAA LRLAEAARYS SLGTFEFLVD AVDTGDDASF AFIEANPRLQ
     VEHTVTEQVT GIDLVMAQLQ LAGGSTLAQL GLTQEEIMPP RGFAIQLRIN MESMQQDGSA
     RPSGGMLTAF EPPSGPGIRV DSFGYAGYTT NPNFDSLLAK LIVHNPSARF DDAIARAYRA
     LCEFRIDGVA TNIAFLQNLL RHPDAVANRV NTRFVEENVE ALLATDGDAH RALYFDSPTN
     DPAPGSKRAQ SAPPGTMPIA APMQGTVVSI DVRESEPVRV GQQIAVLEAM KMEHVVTADK
     SGIVRLVASG KGDVLLEGQA LVFMEDMEIE AVQAEHAQSI DLDHIRADLA EVGERHAVGL
     DAARPDAVAR RRKTGQRTAR ENVDELCDAG SFIEYGALAI AAQRRRRPLD ELIKATPADG
     LIAGIGAING KLFDDDKSRC MVLCYDYTVL AGTQGIMNHK KTDRMFQIAE RSQLPVVIFA
     EGGGGRPGDT DWLGVAGLDV MSFIQFAKLS GLAPRVGIVS GRCFAGNAAL LGCCDVIIAT
     ENATIGMGGP AMIEGGGLGV YSPEEVGPVG MQAPNGVIDL VVGDETEAVR AAKQYLSYFQ
     GPLADWQCAD QRILRQLIPE NRLRVYDIRK VIENLADCDS VMELRRQFGV GIVTALIRIE
     GRPFGLIANN PMYLGGAIDS DAADKAARFM QLCDAFDVPI VSLCDTPGFM VGPDAEKTAM
     VRHVSRMFVT AGSISVPFFT IVLRKGYGLG AQAMAGGSLH ASFFAIAWPS GEFGGMGLEG
     SVRLGFRKEL EAVADLDERK VLFDKMVAAA YERGKAINMA SFLEIDDVID PAESRTWIMR
     GLRSAPKPPS RTGKKRPFID TW
//
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