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
//