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Database: UniProt
Entry: A0A372GC83_9ACTN
LinkDB: A0A372GC83_9ACTN
Original site: A0A372GC83_9ACTN 
ID   A0A372GC83_9ACTN        Unreviewed;      1831 AA.
AC   A0A372GC83;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=ATP-grasp domain-containing protein {ECO:0000313|EMBL:RFS83004.1};
GN   ORFNames=D0T12_22670 {ECO:0000313|EMBL:RFS83004.1};
OS   Actinomadura spongiicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=2303421 {ECO:0000313|EMBL:RFS83004.1, ECO:0000313|Proteomes:UP000262882};
RN   [1] {ECO:0000313|EMBL:RFS83004.1, ECO:0000313|Proteomes:UP000262882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW52907 {ECO:0000313|EMBL:RFS83004.1,
RC   ECO:0000313|Proteomes:UP000262882};
RA   Li L., Lin H.W.;
RT   "Actinomadura spongicola sp. nov., isolated from marine sponge Leucetta
RT   chagosensis.";
RL   Submitted (AUG-2018) 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:RFS83004.1}.
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DR   EMBL; QVNQ01000007; RFS83004.1; -; Genomic_DNA.
DR   OrthoDB; 5166719at2; -.
DR   Proteomes; UP000262882; 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:UP000262882}.
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          576..659
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1552..1828
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   1831 AA;  197932 MW;  1DDD02DE9BBD0B60 CRC64;
     MFSRVAIVNR GEAAMRLIHA VRDIAAETGT RIETVALHTD VDRTATFVRE ADLSYDLGPA
     SARPYLDLKV LERALVESGA DAAWVGWGFV AEDPAFAELC DRIGVTFVGP SADAMRKLGD
     KIGAKLIAEE VGVPVAPWSR GAVETLEAAL RSAAEVGYPL MLKATAGGGG RGIRVISNEA
     ELIDAYERTS QEAARAFGSG VVFLERLVTG ARHVEVQVIA DGQGTAWALG VRDCSVQRRN
     QKVIEESSSP VLSAEQAAEL KASAERLAVA VGYRGAATVE FLYHPGDRLF AFLEVNTRLQ
     VEHPITEATT GFDLVRAQLW VASGGRLDGA PPAERGHAIE ARLNAEDPDR DFAPSPGRIA
     RLVLPAGPGV RVDTGVREGD TIPADFDSMI AKIIAVGRDR AEALARLRRA MAQTTVVIEG
     GATNKSFVLD LLDRPEVIDA SADTGWIDRV RAAGELVSHR HSAVALAAAA IDAYEEEERA
     ERQRLLATAF GGRPQVRHES GRPLDLKLRG VGYRLRVARV GAHRFRVGVE VVGGDEETAR
     TAVVELDRFD RHTGQIVVNG TRYRLLTATH GPVHLVEVDG VTHRVSRDEG GVVRSPAPAL
     VVATPLKVGA EVEAGAPVLV LESMKMETVL RAPFKARLKE CVVSVGAQVE TGAALLRLEP
     LADDAEDAED EATGTVELDL PDGPGTVSAW ERAARCQEEL RSLLLGFDVD PHDEGRVLGD
     YLAAREESGG DRTLAGELEL VEVFTDVAEL GRNRPAGIEV GGAGGGEGSH VHSDREYFHT
     YLKSLDVDRA GLPEAFQAKL TKALGHYGVT GLDRSPELET AVFRLFLAQQ RTSADVRVVA
     TLLRTWLREP PPDQATHEPI GLALERLVAA TQVRFPAVAD LARGVVFAWF AQPLLRRNRA
     RVYADVRRHL RYLDAHPDAP DRADRIAEMV RSTEPLVRLL GRRLVRHDRD NTVMLEVLTR
     RYYGNKGLTG VHTREVGGCE FVVAERADSC VVSAAVGFDA FGGALRGLAE LTGGADAPGA
     DTDADIYLAW ENQPEDFDAM AAALHEVVNA HPLPERVRRL TATVAGSGGA VMHHHFTFRP
     EAGGMVEERL IRGLHPYIAQ RMQMERWSGF DLTRLPSADE EVYLFRGVAR ENPSDERLVA
     FAQVRNLTEL RDHEGRLLAL PTAEYTVAAC LDSIRRAQAL RSSKKRFNTN RVVVYVWPPS
     HLTRAELEMI AGRVLPTTVG AGLEEILFIA RQRDPRTGGL DKIAVRIAFD VTGGAELTVG
     APSDEPVEPV DAYRQKVLGA SSRNTVYPYE LTGLLGDFVE HDLDDANALV PVDRPKGRNT
     AAMVAGVVRT PTARYPEGVT RVVLLGDPTK SLGALSEPEC RRVIAALDLA ERMRVPVEWY
     ALSSGARISM DSGTENMDWV AAALKRIVEF TQDGGEINVV VSGINVGAQP YWNAEATMLM
     HTKGVLIMTP DSAMVLTGKQ ALDFSGGVSA EDNFGIGGHD RVMGPNGQAQ YWAPNLTGAR
     DILMSHYDHT YIAPGETTPR RAPTIDPVDR DIREFPHTVE GSDFSTVGEI FSADTNPDRK
     KPFDIRTVMR ALSDQDHPVL ERWAAMADAD TAVVHDVHLG GIPVCLLGIE SRSVPRRGFP
     PTDGPDSYTA GTLFPQSSKK AARAINAASG NRPLVVLANL SGFDGSPESL RKLQLEYGAE
     IGRAIVNFRG PIVFCVISRY HGGAFVVFSK TLNPMMTVLA VEGSFASVLG GAPAAAVVFS
     RDVDARTAGD PRVRDLEARV GAATGADRAA LTAELDELRS SVRAEKVGEV AAEFDRVHDI
     RRAVEVGSVD AVVRAAELRP RIIEAIESRL R
//
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