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Database: UniProt
Entry: A0A0M4Q477_9PSEU
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ID   A0A0M4Q477_9PSEU        Unreviewed;      1873 AA.
AC   A0A0M4Q477;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   ORFNames=XF36_03820 {ECO:0000313|EMBL:ALE82372.1};
OS   Pseudonocardia sp. HH130629-09.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE82372.1, ECO:0000313|Proteomes:UP000062082};
RN   [1] {ECO:0000313|EMBL:ALE82372.1, ECO:0000313|Proteomes:UP000062082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE82372.1,
RC   ECO:0000313|Proteomes:UP000062082};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules in
RT   bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP011868; ALE82372.1; -; Genomic_DNA.
DR   RefSeq; WP_060710912.1; NZ_CP011868.1.
DR   KEGG; pseh:XF36_03820; -.
DR   PATRIC; fig|1641402.3.peg.813; -.
DR   OrthoDB; 4435847at2; -.
DR   Proteomes; UP000062082; 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; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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:UP000062082}.
FT   DOMAIN          1..462
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          132..330
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          581..660
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1580..1864
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          1543..1568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1873 AA;  203190 MW;  D7C34D77F926E343 CRC64;
     MFSRIAIVNR GEPAMRLINA VREWNAQNGP DRRLRTIALH TAVDRRAMYV READEAVLIG
     PDDPDHMGAS PYLDHAELER ALRVTRADAV WPGWGFVSEK AEFAELCERL GITFVGPSAE
     VMRRLGDKIA SKQLAESVGV PMAPWSGGPV ADVEAARKTA ETVGYPLMVK ATAGGGGRGI
     RYVAGPEQLD EAFERAASEA SRTAGDATVF LERAVSGGRH VEVQVVADAT GDVWTLGVRD
     CSVQRRNQKV IEESASTALD PTQEELLRSS AAELARAAGY VNAGTVEFLY QPEEKLLSFL
     EVNTRLQVEH PVTEACTGVD IVKLQLHVAA GGTLAEVARE VPAAQGWAIE ARLTAEDPER
     EFAPAPGRIE HLALPSGPGI RVDTGVAAGD VIPPQFDSMI AKVIAWGRDR DEARARLSRA
     LRQTAAVIDG GSTNKAFLLD LLDRDEFRSG ELQTTWLDGM MAEGYAPPRR LDVALLATAV
     LSHDGHVARQ QERLFRSAEA GRPEVGYETW HQTDVTVAGQ SYKLKVARTR AGRYTVELDG
     TSVDVDVERN GAYERRLTVG DRSWTVLSVA QEADYLVEVD GAVHRISGGE AGIVRAPAPA
     MVVALPVTAG QTVAEGDTLA IVESMKLETS LRAPFDGTVA EILVPANTQV DGGTKLVRLE
     PSADADAAAP SGERADLSAF AATGADTDPA ATAADALSAL RFQVLGFDVD ERQARPQLRR
     LAGAREQLAA DDPAVLAGET AVLQIFADLC QLSRNRSETD DETGETERNP QEYLYAYLRS
     RDAEDEGLPE SFQAKLRRAL AHYGVAEIDG GAARADDLGP ALYRMFLAHR RAPQQVPVVL
     DLLNWRLRHP ESVAHLSPAA REDYLRTLDE VVVATQLRHP VVGDTARLVR YRAFDAPVVA
     AERDRALAEV RESLDVLAEN PDADDRARRI AALVGSSEPI LGVFGERHDA VLLEVMTRRY
     YRVRVLRDLE LVEHAGKPLL TARYQHLGRD RTLFASVIDN NDPAAAQAVA DELRRRVGEL
     DGDRTALVDL YVTSTKADDG GDPDARAERV RAALGKVPAN LHRVAVAVRP NPRAAGTASE
     EAEPPTWFTF RPDETGELVE DRTLRGMHPL VADRLRLWRF RDFELHRLPA ATDVHLFRAT
     GREVTADDRL VAMANVRELT VLRDEETGKV RSLPQFERAL DACINSLRAA RAGDRTLARM
     SWNRIALYVW PEVDVPLAEL DSVVRRLAPR TANLGLEQVL VEFRTADPQV TGGQGGPRSM
     LLRMSRPPGA GLQVKLDQPP TEPMRELDAY DQKVLKARRR GAVYPYEIVP LLTAPIDAGP
     GTWQEYDLVD PDDPALPVPV DRAPGGNTAN LVLGVVSVPT RRYPDGMKRV VLLGDPTRAL
     GAIAEPECRR VLAAIHLARE LDVPIEWFAV SAGAKIAMDS GTENMDWISR VLRGIIEFTQ
     DGGELNVVVT GINVGAQPYW NAEATMLMHT KGILVMTPDS AMVLTGKHSL DFSGGVSAED
     NFGIGGYDRI MGPNGQAQYW APDLSGAVGV LLAHYAHTWT QPGERFPRPA PTTDPVSRDV
     TTAPHSGPNC EFTTLGEIWA PETNRERKKP FDIRSVLRGV ADADHPTSER WADMHDAESV
     VALDAHLGGQ PIAMIGIESR PLPRRGPRPV DGPSQFTAGT LFPRSSRKCA RAINAASGNR
     PLVVLANLSG FDGSPESLRG LQLENGAEIG RAIVNFDGPI VFCVVSRYHG GAFVVFSGTL
     NDNMEVAAIT GSYASVLGGA PAAAVVFAGE VNDRTAKDER ITDLEARITR AVTDGDEATA
     ARLRGDLATL RPDVRSEKLG QVAEEFDTKH SIERARSVGS VHRIVSPDQL RPYLADAVQR
     GMKRTLDTLG GTA
//
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