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Database: UniProt
Entry: A0A127MI11_9SPHN
LinkDB: A0A127MI11_9SPHN
Original site: A0A127MI11_9SPHN 
ID   A0A127MI11_9SPHN        Unreviewed;       451 AA.
AC   A0A127MI11;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00017242, ECO:0000256|RuleBase:RU365063};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE   AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|ARBA:ARBA00033786, ECO:0000256|RuleBase:RU365063};
GN   ORFNames=AZE99_14715 {ECO:0000313|EMBL:AMO72934.1};
OS   Sphingorhabdus sp. M41.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO72934.1, ECO:0000313|Proteomes:UP000073959};
RN   [1] {ECO:0000313|EMBL:AMO72934.1, ECO:0000313|Proteomes:UP000073959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M41 {ECO:0000313|EMBL:AMO72934.1,
RC   ECO:0000313|Proteomes:UP000073959};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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|ARBA:ARBA00003761, 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] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000256|RuleBase:RU365063};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956,
CC       ECO:0000256|RuleBase:RU365063}.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl
CC       carrier protein, biotin carboxylase and the two subunits of carboxyl
CC       transferase in a 2:2 complex. {ECO:0000256|ARBA:ARBA00011750,
CC       ECO:0000256|RuleBase:RU365063}.
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DR   EMBL; CP014545; AMO72934.1; -; Genomic_DNA.
DR   RefSeq; WP_067202680.1; NZ_CP014545.1.
DR   AlphaFoldDB; A0A127MI11; -.
DR   STRING; 1806885.AZE99_14715; -.
DR   KEGG; sphg:AZE99_14715; -.
DR   OrthoDB; 9763189at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000073959; Chromosome.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; TIGR00514; accC; 1.
DR   PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365063};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU365063};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          2..445
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          121..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   451 AA;  49539 MW;  CF5CA466AEE31D74 CRC64;
     MTIEKILIAN RGEIALRILR AAKELGIETV AVHSTADADA MHVRLADQAV CIGPPPAADS
     YLSIPAIISA AEISGADAIH PGYGFLSENA HFAEVVEAHG IKWIGPKPEH IKIMGDKVAA
     KKTAGDLGIP LVPGSDGAVS EIEEAKQVAR QVGYPVIIKA ASGGGGRGMK VVNSETELET
     QMKQAGTEAK AAFGDATVYI EKYLGDPRHI EFQVFGDGRG NAIHLGERDC SLQRRHQKVL
     EEAPSPVISA EQREKMGKVC VDAMKGMSYR GAGTIEFLYE NNEFYFIEMN TRLQVEHPVT
     EMITGFDLVR EQIRIADGRD LSVTQDELEF KGHAIECRIN AENPKTWAPS PGKVTSYHAP
     GGMHVRVDSG LYAGYSIPPY YDSMIAKLIV YGRTRDGCMM RLARALDEFV IEGVQTTIPL
     HQKLVYDEEF QSGEYTIKWL EEWLEKDNLK D
//
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