ID C7PW61_CATAD Unreviewed; 1816 AA.
AC C7PW61;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding {ECO:0000313|EMBL:ACU73309.1};
GN OrderedLocusNames=Caci_4446 {ECO:0000313|EMBL:ACU73309.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU73309.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU73309.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP001700; ACU73309.1; -; Genomic_DNA.
DR STRING; 479433.Caci_4446; -.
DR KEGG; cai:Caci_4446; -.
DR eggNOG; COG4770; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_239133_0_0_11; -.
DR InParanoid; C7PW61; -.
DR OMA; NTVYPYE; -.
DR Proteomes; UP000000851; Chromosome.
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 CARBOXYL CARRIER PROTEIN; 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:UP000000851}.
FT DOMAIN 1..438
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 111..309
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 562..645
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1534..1816
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1816 AA; 196868 MW; 95D43FA9E45ABF66 CRC64;
MRLIHAVREL SAQSATPIET VALHTDVDRD ATFVREADIA FDLGPAAARP YLDLKVLEHA
LLESGADAAW VGWGFVAEDP AFAELCDRIG VTFIGPDAEA MRQLGDKIGA KLIAEEVGVP
VAPWSRGAVE TLETAIEAAG QIGYPLMLKA TAGGGGRGIR VITNESELVD AYERTSQEAA
RAFGSGIVFL ERLVTGARHV EVQVIADGQG TAWALGVRDC SIQRRNQKVI EESASPVLSA
EQAAELKSSA ERLAVRVGYR GAATVEFLYH PGDKQFAFLE VNTRLQVEHP ITELTTGFDL
VKAQLHVAGG GKLEGRPPAE RGHAIEARLN AEDPDRDFAP SPGRIARLDL PAGPGIRVDT
GVSEGDTIPA DFDSMIAKVI AYGRDRDEAL GRLRRAMAET SVVIEGGTTN KSFVLDLLDQ
PEVIDASADT GWIDRVRAEG RLVSHRNAAV ALAAAAIDAY EDEERVERAR LLSTASGGRP
QVQHESGRPL DLKLRGVSYK VRVARVGAHR FRVGIEAGDG HGAQSQTADV VLDRFDRHTG
QIAVNGSRFR LLTATHGSVH QVEVDGVTHR VSLDEGGVIR SPAPALVIAT PLQVGAEVEA
GAPVVVLESM KMETVLRAPF KARLKELAVT VGSQVETGAP LLRLEQIVEE DADEAAASAS
AQPTEAAELD LPAAPAEVPV RARVAQGQED LRSLLLGFDV DPHDEDRILA GYVEARTTAV
EQGLRPLSGE LSLIEVFADL ADLGRNRPAA AAEESNGESQ LHSAHEYFHT YLQSLDVERA
GLPESFQAAL RKVLAHYGVT ELDRSPELEA AVFRIFLARQ RSATDATVIA ALMRAWLREL
PPDELLREPT GLALERLIAA TQVRFPNVAD LARGVVYAWF GQPLLRRNRA RVYAAIRKNL
RYLDENPRAE DRDERVAEMV RSTEPLVRLL AQRLVHTELD NSAMLEVLTR RYYGNKGLTG
VRTTEVGGNP FIVAEHDGSQ LASAAVPFDR LGDALDGLAE LAASAGALDA DIYLLWENQP
DTDEAATALQ RVISAHPLPQ QVRRVTATVA GRRNSVMHHH FTFRRSTTGL TEERLIRGLH
PFIAERMQLE RLNKFDLTRL PSSDEDVYLY QCVARENPAD DRLVAFTQVR DLTELREHDG
RLVALPTAED AIAACVDSIR RAQLRKPSNK RFSTNRVVVY LWPVSDIKRS ELYLIAQRIL
PSTVGAGLEE IELIGRQRSW KTGELIKIAV RVRFDTAGNP SLNVGEPTLS PIEPLDDYRL
KVMRAASRGT VYPYELVDSL GDFTEHDLDE AHTLVPVDRP KGRNSAAMVA GVISTKTRRH
RQGVTRVLLL GDPTKSLGAL SEPECRRVIA ALDLAEQMKV PVEWYALSSG ARISMQSGTE
NMDWVAAALK RIVEFTQDGG EINVVVNGIN VGAQPYWNAE ATMLMHTRGV LVMTPDSAMV
LTGKQALDFS GGVSAEDNFG IGGYDRVMGP NGQAQYWAPS LAAARDVLMS HYDHTYIAPG
ETSPRRAGTD DPYDRDVSSF PHTFAGSDFT TVGEIFSAAA NPDRKKAFDI RTVMRALSDQ
DHPVLERWAG MAGAETSVVQ DVHLGGLPVC LVGIESRAVP RRGFPPTDGP DTYTAGTLFP
QSSKKVARAI NSASGNRPLV VLANLSGFDG SPESMRKLQL EYGAEIGRAI VNFEGPIVFC
VISRYHGGAF VVFSKALNPN MTVLALEGSY ASVLGGAPAA AVVFSGDVNS RTANDPRIRD
LESRVTAASG TDRAALAAEL DELRASVRAE KLGEVATEFD RVHSIQRAVQ VGSVDEVIKA
ADLRPKIIAS IEARLG
//