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Entry: A0A1Z4BYU0_9GAMM
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ID   A0A1Z4BYU0_9GAMM        Unreviewed;       447 AA.
AC   A0A1Z4BYU0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
DE   RecName: Full=Biotin carboxylase {ECO:0000256|RuleBase:RU365063};
DE            EC=6.3.4.14 {ECO:0000256|RuleBase:RU365063};
DE            EC=6.4.1.2 {ECO:0000256|RuleBase:RU365063};
GN   Name=accC {ECO:0000313|EMBL:ASF46419.1};
GN   ORFNames=AADEFJLK_00829 {ECO:0000313|EMBL:POZ53788.1}, CEK71_10210
GN   {ECO:0000313|EMBL:ASF46419.1};
OS   Methylovulum psychrotolerans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylovulum.
OX   NCBI_TaxID=1704499 {ECO:0000313|EMBL:ASF46419.1, ECO:0000313|Proteomes:UP000197019};
RN   [1] {ECO:0000313|EMBL:ASF46419.1, ECO:0000313|Proteomes:UP000197019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HV10_M2 {ECO:0000313|EMBL:ASF46419.1,
RC   ECO:0000313|Proteomes:UP000197019};
RA   Mateos-Rivera A.;
RT   "Genome Sequencing of the methanotroph Methylovulum psychrotolerants
RT   str. HV10-M2 isolated from a high-altitude environment.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:POZ53788.1, ECO:0000313|Proteomes:UP000237423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sph1 {ECO:0000313|EMBL:POZ53788.1,
RC   ECO:0000313|Proteomes:UP000237423};
RA   Oshkin I.Y., Miroshnikov K., Belova S.E., Korzhenkov A.,
RA   Toshchakov S.V., Dedysh S.N.;
RT   "Draft Genome Sequence of Methylobacter psychrotolerans Sph1T, an
RT   Obligate Methanotroph from Low-Temperature Environments.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA.
CC       {ECO:0000256|RuleBase:RU365063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000256|RuleBase:RU365063};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000256|RuleBase:RU365063};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1. {ECO:0000256|RuleBase:RU365063}.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin
CC       carboxyl carrier protein, biotin carboxylase and the two subunits
CC       of carboxyl transferase in a 2:2 complex.
CC       {ECO:0000256|RuleBase:RU365063}.
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DR   EMBL; CP022129; ASF46419.1; -; Genomic_DNA.
DR   EMBL; PGFZ01000001; POZ53788.1; -; Genomic_DNA.
DR   KEGG; mpsy:CEK71_10210; -.
DR   KO; K01961; -.
DR   BioCyc; GCF_002209385:CEK71_RS10210-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000197019; Chromosome.
DR   Proteomes; UP000237423; Unassembled WGS sequence.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00514; accC; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|RuleBase:RU365063};
KW   Biotin {ECO:0000256|RuleBase:RU365063};
KW   Complete proteome {ECO:0000313|Proteomes:UP000197019,
KW   ECO:0000313|Proteomes:UP000237423};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Ligase {ECO:0000256|RuleBase:RU365063};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|RuleBase:RU365063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197019}.
FT   DOMAIN        1    445       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   447 AA;  48855 MW;  FF69ABBA277BE13C CRC64;
     MFDKIVIANR GEIALRILRA CRELGVKVVA VHSEADRDLK HVRLADESVC IGPAASADSY
     LNIPAIISAA EVTDAEAIHP GYGFLSENAD FAEKVKQSGF VFIGPNADTI RMMGDKISAK
     NAMLAAGIPC VPGNNDPLSD DNKKNLKLAQ EIGYPVIIKA AGGGGGRGMR TVHTEAALIN
     AIAMTKAEAG SAFGNPTVYM EKFLEDPRHI EFQVMADSYG NAIHLGERDC SMQRRHQKVV
     EEAPAPGITE EQRRLIGERC AKACIDIGYL GAGTFEFLYE KGEFYFIEMN TRVQVEHPVT
     EMVTGFDIVK EQLRIAAGER LSITQDQVKI QGHAIECRLN AEDPQTFMPC PGKIEQFHMP
     GGPGIRCETH IYNGYKVPPY YDSMIGKLIA HGETRSSAIA RMNTALSEII IDGIKTNIPL
     QQDIMNDSAF AAGGQNIHYL EKKLGLY
//
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