ID D2S4A4_GEOOG Unreviewed; 1843 AA.
AC D2S4A4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding protein {ECO:0000313|EMBL:ADB75094.1};
GN OrderedLocusNames=Gobs_2423 {ECO:0000313|EMBL:ADB75094.1};
OS Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB75094.1, ECO:0000313|Proteomes:UP000001382};
RN [1] {ECO:0000313|EMBL:ADB75094.1, ECO:0000313|Proteomes:UP000001382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RX PubMed=21304698;
RA Ivanova N., Sikorski J., Jando M., Munk C., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Meincke L.,
RA Brettin T., Detter J.C., Detter J.C., Rohde M., Goeker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Geodermatophilus obscurus type strain (G-
RT 20).";
RL Stand. Genomic Sci. 2:158-167(2010).
RN [2] {ECO:0000313|Proteomes:UP000001382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP001867; ADB75094.1; -; Genomic_DNA.
DR RefSeq; WP_012948529.1; NC_013757.1.
DR STRING; 526225.Gobs_2423; -.
DR KEGG; gob:Gobs_2423; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG4770; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_239133_0_0_11; -.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000001382; 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 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; 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:UP000001382}.
FT DOMAIN 1..453
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 573..652
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1546..1824
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 655..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1843 AA; 199895 MW; 4368B19DDEE85221 CRC64;
MFDRIAVVNR GEPALRLIRA VRELNAEHGT RTRVVALHTE AERRATFVRA ADEAVLLDDS
GGGSPYLDHA ELARALRVSG ADAAWVGWGF VAEDPAFAEL CADLGVTFVG PPPEAMRLLG
AKIEAKVLAE KVGVPVAPWS HGPVESLDDG RRHADVIGYP LIVKARSGGG GRGIRVVRSP
DELEEALTRT RSEAEKSFGD PIVFMERLVE GGRHVEVQVI ADQHGTVWAP GVRDCSVQRR
NQKVIEESSS PALTGEQDAA LRESAVALVR AAGYVGAGTV EFLYQPEEQL TTFLEVNTRL
QVEHPVTELT TGLDLVKLQL HVAAGGRLEG RPPEANGHAV EARLTAEDAE QGFAPAPGRV
ELLRLPTGPG VRVDTGISVG DVIPPQYDSM IAKVIGWGRD RSEALARLRC ALQETTVVLR
GGTTTKSFLL DLLDRPEVVS GTADTGWLDR AGSVGAPRAS ETAWVALVQV AVDLAEAEEE
QERLAFLASA RGGRPRAPHE VGRTIELGMR GQVYRLTVAT VDRDRYRVGL DGRVVDVEVD
RLGPLESRLS IGGRRYSVVA AQAPGSSLVE VDGETHRVSR DVGGVVRAPA PAVVVAVRAG
VGDEVEAGQP IAVLESMKME TAVRAPFAGR VREVRAAVNS QVDAGAPLLT LERTGGDVEE
ATGERVTLPD ADETPDGDPR ARALDRLAAL RALVTGYDVS GRHAKRLVAE YATARDELPA
DDAQLLHAEL DVLVTFADIS ELSRNRPASA EEEAETQVHS PREYFQAYLR SLDVEREGLP
EAFRARLRRA LAHYGIEDLE PSAALTEAVH RIFLAQQRVA EQLPAVSALL DRWLTADQLP
EGPARAEVGE VLDRLVVATQ LRYPSVGDMA RAVRYRHFEE PVVRAARQEV LDRAARLLDE
LDEAGARGDT AESIRRMEAL VASPEPLVRL LAQRFDRATS VPDPVLEVLT RRYYRSRSLE
DVRSTLLDGD TCVTAEFDLH GNRLHLLALM TDHARLPEAL GSVAGALADV ADPTQVVVDL
YLNWPDRPAD DDEVSERLRG QLEGVPALRT GRRVTVTVCT PDGEVETITF RPTPDRAQSP
TGRSGPATGL AEERVIRGLH PLTAQRLDIW RFKEFDGERV PSPEDTYLLH ITAKENPNDE
RFIAMAEVRD LTPVRDEHGA VVGFPTIERQ LTSCLDGLRR AQSLRRSRRP LENNRIHLYA
WPSIEVPLAE VAEFARTAAP LTYGAGLDQI VLLARLPEEG GPPRDVALRF SARPGTGVQM
RVTDRPTEPL RVLDDYTAKV LSSRARGAPY PYELAPLLAG SDGSFVEHDL DADGRLAPVE
RPPGQNKAGI VVGLVTTPTP RYPEGMTRVA LFGDPTKALG TVAEPECARV VAALDLAEER
DIPVEWFALS SGARISMDSG TENMDWVSRA LRRIIEFTQA GREINVVVTG INVGAQPYWN
AEATMLMHTK GILVMTPDSA MVLTGKHSLD YSGGVSAEDN FGIGGYDRVM GPNGQAQYWA
PDLNGALDVL FRHYDHAYRA PGERWPRPAQ TSDPRDRDVR SFPHTHPDSE FTTVGDVFSA
EANPERKKAF DIRTVMRAVT DQDHPVLERW AGMADADTSV VLDAHLGGHP VTVLGVESRP
IPRRGSHPAD GPDQWTAGTL FPRSSKKTAR AINAASGNRP LVVLANLSGF DGSPESLRNI
QLEYGAEIGR AITNFDGPIV FCVVSRYHGG AFVVFSGVLN DNMEVLAVEG SYASVIGGAP
AAAVVFAREV DKRTAADPRV KELEAAIAAA DAVEQAHLRS QLATLRSAVR SEKLGEVAAE
FEAVHDIERA RRTGSVHAII PAAELRPRLI AAVERGMDRA ATT
//
