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}.
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; 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
//