ID M0QQT7_9ACTN Unreviewed; 1822 AA.
AC M0QQT7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative acyl-CoA carboxylase {ECO:0000313|EMBL:GAC69792.1};
GN ORFNames=GS4_28_00400 {ECO:0000313|EMBL:GAC69792.1};
OS Gordonia soli NBRC 108243.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC69792.1, ECO:0000313|Proteomes:UP000011666};
RN [1] {ECO:0000313|EMBL:GAC69792.1, ECO:0000313|Proteomes:UP000011666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC69792.1,
RC ECO:0000313|Proteomes:UP000011666};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia soli NBRC 108243.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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:GAC69792.1}.
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; BANX01000028; GAC69792.1; -; Genomic_DNA.
DR RefSeq; WP_007623208.1; NZ_BANX01000028.1.
DR STRING; 1223545.GS4_28_00400; -.
DR eggNOG; COG4770; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000011666; 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:UP000011666}.
FT DOMAIN 1..452
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 572..655
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1514..1815
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1822 AA; 197606 MW; FB4805F11EB0E5A3 CRC64;
MFTRIAIVNR GEAAMRLIRA ARAMSAETGQ HIEVVALHTD VERTATFVRD ADITYDLGPA
ANRPYLNLKT LERALLETGA DAAWVGWGFV AEDPRFAELC ERIGITFVGP SPEAMRKLGD
KIGAKLIAEE VGVPVAPWSG GAVDSVDDAK AAAARIGYPL MLKATAGGGG RGIRVITSDD
ELVDAYERTR AEAERAFGSG VVFLERLVTG ARHVEVQVIA DGQGTAWALG VRDCSVQRRN
QKIIEESASP VLAPEQAEEL KRSAERLALA VGYRGAATVE FLYHPGEKLF AFLEVNTRLQ
VEHPITESTT GFDLVRAQLS VAAGVPLSGE MPRERGHAIE ARLNAEDPDR DFAPAPGRIA
RLDLPTGPGI RIDTGVSEGD VIPADFDSMI AKIIAVGSDR EEALGRLRRA MSETRVVIEG
GATNKSFVLE LLDRPEVIDG SADTGWIDRV RAADGLVVNR HATIALAASA IDAYEEEESV
QRSRLLATAA GGRPQVQHRS GRPLDLKLRG VGYRVRVARI GAHRFRVVIE AGDQSRTADV
DLDRFDEHTA QMVLNDVRYR LLMDTHGPVR FVEVDGIAHR VSLDEGGVLR APAPALVVAL
PVEVGTEVEA GAPVLVLESM KMETVLRAPT RSRLRECTVS VGSQVEVGAP LLRLEPLSDD
TDDEAHAPVE VADLELPEPA QLDAADRTTR TQEDLRSQLL GYDVDPHDRS RLLHDYLNVR
RVAAQGGRRP LADEIELIDV FADLAQLSQN RLSDEELGVE HVHSARENFH TYLQSLDVDR
DGLPAAFHDQ LLRALRHYGV TDLDRSPDLE AAVFRIFLAL QNPADSVTVV SALLKEWLAE
PTPRDELRDD VAAGLDGLVA ATQVRFPAIA DLARAVVYAW YGQPLLRRNR ARIYNDVRKQ
LRHLDGAPDS SDRDERIAAM VRSTEPLVRL LGQRIERGHL DNTVMLEILT RRYYGNTGLK
SVRTHQAGGT TFVVAERDGV QLASAAVSFD NVAAAVGGLV ELAKDTSSMD ADIYLSWEQQ
PDSFDEMARV LHDIVTANPG PHQLHRLTFA VAGSGNARMH HHFTFRPSAT GMVEERLIRG
LHPHIARRMQ MERLRKFDLT RLPSSDDEEV YLFRCVAKEN PADDRLIAFA QVRDLDALRE
HDGRLMTLPT AETTLASCVD SIRQARADGK RTSDTNRIVM YVWPPIGTAP ADLQTISDHI
WATTRGVGIE EVLLIARRRD RVSGTLEKVT VRFSVTATGG FDVVVGDPTD EPIEPVDSYR
QKVLRAARRN TVYPYELVDL LGAFTEHDLD DAGQLVPVDR PRGNNSAAIV AGIVTTPTAK
HPDQGVTRVL LLGDPTKSLG ALSEPECARV IAAIDLADRL GVPVEWYALS SGARISMDSG
TENMDWVAKA LKRVVEFTQA GGEINIVVAG INVGAQPYWN AEATMLMHTK GVLVMTPDSA
MVLTGKQSLD FSGGVSAEDN FGIGGYDRVM GPNGQAQYWA PNLAAARDVL MSHYDHTYVA
PGEAGPRRAT TTDPVDRDVR DFPHVLAGSD FTTVGDIFSV ATNPDRKKPF DIRTVMRAVA
DQDHQVLERW AGMADAETAV VADVHLGGIP VCLLGIESQE VQRRGYKPTD GPDVYTAGTL
FPQSSKKAAR AINVASGNRP LVVLANLSGF DGSPESMRKL QLEYGAEIGR AIVNFRGPIV
FCVISRYHGG AFVVFSKALN PNMTVLAIDG SFASVLGGAP AAAVVFAGEV ASRVAADPRV
RAVEARMAEA AGAELPALNA ELADVRQSVR AEKISEVAAE FDGVHSIRRA VEVGSVDAVI
GADELRPRII AAIAGFGGAA DS
//
