ID N0E4J4_9MICO Unreviewed; 1870 AA.
AC N0E4J4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding protein {ECO:0000313|EMBL:CCH69944.1};
GN ORFNames=BN10_460045 {ECO:0000313|EMBL:CCH69944.1};
OS Phycicoccus elongatus Lp2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1193181 {ECO:0000313|EMBL:CCH69944.1, ECO:0000313|Proteomes:UP000013167};
RN [1] {ECO:0000313|EMBL:CCH69944.1, ECO:0000313|Proteomes:UP000013167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lp2 {ECO:0000313|EMBL:CCH69944.1,
RC ECO:0000313|Proteomes:UP000013167};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH69944.1}.
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DR EMBL; CAIZ01000115; CCH69944.1; -; Genomic_DNA.
DR STRING; 1193181.BN10_460045; -.
DR eggNOG; COG4770; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_239133_0_0_11; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000013167; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
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; PTHR18866:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR Pfam; PF08326; ACC_central; 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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000013167}.
FT DOMAIN 39..494
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 167..365
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 613..696
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1591..1870
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1558..1581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1870 AA; 200703 MW; 3DDB647ABAD892B2 CRC64;
MPGHLLRPVS GRQSNHFAGR RVITRELPGS HDSLTRVTTF SRIAVVNRGE AAMRLIHAVR
DLNAATRQTG GHQIEVIALH TEGEKRAMFV READVAYDLG PAANRPYLDH ALLERALTQT
RADAAWVGWG FVAEDAAFAD LCARIGVAFI GPSGEAMRKL GDKIGSKLIA EEVGVPVAPW
SKGGVETLGD ALAVANDLGY PLMLKATAGG GGRGIRKVSS DDELTAAYQL TREEAQRAFG
SGVVFLESLV TGARHVEVQV IADGQGTAWA VGVRDCSVQR RNQKVIEESA SPVMTRDQAQ
LLKDSAERLA IAVGYAGAGT VEFLFQPQDG TFAFLEVNTR LQVEHPITEE VTGLDLVKLQ
IHVAQGGRLE GERPAENGHA VEARLNAEDP DRDFAPSPGH ISLLELPAGP GIRVDTGVGE
GDSIPADFDS MIAKIIAWGR DRDEALARLR RAMDETTVVI EGGSTNKSFI LDLLAQPEVI
DGSADTGWID RVRGEGRLIA HQHSGVALVA AGIEAYLDEE AVERARLLET ARGGRPQAQH
RVGQSVDLKL RGAAYKVTVL RIGPHRFRVA ITGAGTATVD ADLDVINDYA SRIRIGDRTH
RLVTATHGPT QLVEVDGVTH RVSRDEGGVL RSPAPALVVA TPASTGDELA EGAPAIVLES
MKMETVLPAP FAGVVREVLV AAGHQVETGA PLLRIDPVVD DEGAEAAPAA AEESVDLDLA
YEAADGSDAL AQGRADIEAM LLGYDVDPQD DGGTLQRYLA ERERRQGDSG LTSEELDLLE
VFADFAELSR NRPVGDDEHS ENQVHSPREH FHTYLQSLDA ERGGLPEAFR SKLARVARHY
DVSSLDRSPE LEAAVFRIFL AQQRSTPDVL IATALLQEWI DEPPPSGDLG DRARDVLDRL
VVATQLRFPV VGDLARSVRF RWFDQPGVDE DRSSVLARVG PEIEAIAGLP TGDERSARLD
ALAGIPERIV SFLGRRFENG LPETEPMLAV LIKRHYHEHA ISEVGETQIH GRPFATADYT
LDGRYSHLVS TIANHDELTP DSEFTADLTA QVESREEGVE GVVDLYLHWP EAPASDDEAS
AQLAATLAAL PVTHTVRRIA VGVAPGDARE VGYFTFRPAG DGALTEDLLV RNVHPMVGRR
LNLWRLRDFD LTRLEGPTDV LLLKGQAKGN AADQRLFALA QVRQFSVARD EAGNVVALPH
LERAIANCLE GIRRARAAAG SGGARLDMNH VWLHVWPPVS ADLDQLTALE SRIAPMTAGA
GIEELRIEGR LAGAGGSITP IVVKFRALPG SGIVTTFEEP ATERLAPLDG YAEKVVRARR
RGLVYPYELV SMVAGGGGTA VEHDLDASGR LVPVDRPYGQ NTAGIICGVV TTPTGLHPEG
VTRVLLCGDP LRSLGSVAEA ECARIMAAID LAEEMGVPVE WFALSAGARI AMDSGTENMD
WIAKALRRIV DFTQAGGEIN VVVAGINVGA QPYWNAEATM LMHCKGVLIM TPDSAMVLTG
KQSLDFSGGV SAEDNFGIGG YDRVMGPNGQ AQYWAKDLAE AYGILLEHYD HTWVAPGEAT
PRRAQTSDPT DRDVTAYPHD PKDSGFTTVG DIFSKQTNPD RKKAFDIRTL MRSVTDQDHP
MLERWAGMAD AETSVVTDAH IGGIPVCLIG IESKSVARRG FPPTDGPDSY TAGTLFPKSS
KKTARGINAA SGNRPLVVLA NLSGFDGSPE SMRKLQLEYG AEIGRAIVNF KGRIVFVVVS
RYHGGAFVVF SKALNDDMTV LAVEGSFASV IGGAPAAAVV FARDVDARTA KDPRVADLED
QVRNAAGSQR AGLVAQLDET RQAVRAEVLG QVASEFDGVH SIHRAVEVGS VDEVIAARDL
RPRIIAALES
//
