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Database: UniProt
Entry: Q1N4X3_9GAMM
LinkDB: Q1N4X3_9GAMM
Original site: Q1N4X3_9GAMM 
ID   Q1N4X3_9GAMM            Unreviewed;      1621 AA.
AC   Q1N4X3;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=Acetyl-CoA carboxylase multifunctional enzyme accADC, carboxyl transferase subunit alpha/carboxyl transferase subunit {ECO:0000313|EMBL:EAT13305.1};
GN   ORFNames=RED65_01055 {ECO:0000313|EMBL:EAT13305.1};
OS   Bermanella marisrubri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Bermanella.
OX   NCBI_TaxID=207949 {ECO:0000313|EMBL:EAT13305.1, ECO:0000313|Proteomes:UP000004263};
RN   [1] {ECO:0000313|EMBL:EAT13305.1, ECO:0000313|Proteomes:UP000004263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RED65 {ECO:0000313|EMBL:EAT13305.1,
RC   ECO:0000313|Proteomes:UP000004263};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (MAR-2006) 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}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC         CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC         Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00001072};
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:EAT13305.1}.
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DR   EMBL; AAQH01000002; EAT13305.1; -; Genomic_DNA.
DR   RefSeq; WP_007017689.1; NZ_CP051183.1.
DR   STRING; 207949.RED65_01055; -.
DR   HOGENOM; CLU_003206_0_0_6; -.
DR   OrthoDB; 9763189at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000004263; Unassembled WGS sequence.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:InterPro.
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   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; IPR001095; Acetyl_CoA_COase_a_su.
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; 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; 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; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   PRINTS; PR01069; ACCCTRFRASEA.
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; PS50989; COA_CT_CTER; 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:UP000004263};
KW   Transferase {ECO:0000313|EMBL:EAT13305.1}.
FT   DOMAIN          53..273
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   DOMAIN          1042..1494
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          1166..1362
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   1621 AA;  181202 MW;  666E520CDF725AAE CRC64;
     MSQYDTDQLF QIAEKLSQDF SLFPEQDGKA NSISGLVSPD KIEETRENLR SLGIDEYIQE
     VVSPSESSTR LNARQLLHKL THRFISEQEW GPLYVAEVEL PFGKQYRRVG FICQNRAERN
     GAWLPEHHKQ AIKAVHQFSR HAIPIVTFID TPGADASEEA NLNNQAHSIS HLIAEMTNTD
     VPTVGVILGA GYSGGAIPLA ATNILLSVRD GIFNTIQPQG LASIARKYNL SWQECAKYVG
     VSAYELLEKH AIDGIIDYAP SDRIDKVQNL LKAITSSISG IETSVLNFAK ENPYLFDHYK
     RSVERFLNPS DKLSAIERTS SLVLASSPTE HHNLFRMTYR YMRYLTLRSR ISSKTKGAYS
     RLAEVEIPKG KLNERIAEEK RKNFQQWLQA PDQLRYDDEL NKLWKNYCQK FKERDEERGS
     ISKLFFGEPE DNYIKAKQEL SFALGLYLFN RWKADASVNF KELIDYLSNY EESRFLIKRK
     DLTDAQAIIG FIKKGEHPLA TFIHQSLDYD TQALLADYTN EKETSADLTS GLTEAFNRII
     SQEPIPESVY GEIKLKEVTQ QLVHNVAASY MEANRRIIED ALAPYISIKT DEILEDNNQD
     ANVLDAILMD DLRTDFIGIC QNLIMFGSLY DYVIANLVTV AKEAKETHSL SVNAVKQLLE
     GGLEHANKLS IADDHHEEFA NWFQYFINSN SKAEFLKQVE EWKKHSFPRL SDTLFVIVTF
     FFEKLLPEYY QAKDGKEYNG RINPYSIGRK KDFWNRLTIA YFDLLIQDVL DDVKRQKTTS
     VQAIIDQFFH DFEEINEHLI TADPVNFPGF RSSIEKALSN DQTPCGVVTG FGTITIGDES
     RRVGTLISNL DFQAGAFDMA SAEKFCKLLV ECARHNYPIV CFVSSGGMQT KEGASALFSM
     PIVNDRITRF VRDNDLPVVV FGYGDCTGGA QASFVTHPMV QTFYFSGTNM PFAGQIVVPS
     YLPSTSTLSN YLSNNQGAMA DLVKHPFVED LDSRLRAIDP AIPVAHKTVN EVLQRILKGY
     VTPAKAKPQE QNEGLNKKLF NPVKKVLIHA RGCTADKLVK KAQDNNISVV LVQSDPDMNS
     TAADRLSSKD RLVCIGGNTP DESYLNAQSV IRIAQLEKVD GLHPGIGFLS ESAQFAAFCE
     NNNINFIGPR VSSMETMGNK SNAINTAISV DVPVVPGSHG IVTTSAKAAK VADKIGYPVL
     LKAVHGGGGK GIQVVREPGE IHELFHQIST EARSAFGNGD VYLEKFVTSL RHIEVQVLRD
     GHGNCKVLGL RDCSVQRNNQ KIIEESGSVT LPDTLEKKVY DYARKLADAV DYVGAGTVEF
     IYDLDANDVY FMEMNTRLQV EHPVTELVTG VDIVSEQFNI ASGGNIEKLT FKEKGYAMEL
     RINAEKARQS GDDVTFVPNA GKITAFNLPE AGHIQIIKAI DENKEVTPFY DSMVVQLICY
     GKDRNDTIKK LLAYLDDVVI EGVSTNIPLL KRILADDVFV KGVYDTNYLP QFLQRIDQTA
     LIEEIDASAG AASAALTVDA LKIDGSSELK VLAPSSSIYY SAPSPSEPSY IKEGDVISTN
     QTLCLMEAMK MFSPLTLRSF NNQGSKLYDT EQNYQVVRIQ NSDGQQVNQG DLLFVIRPVT
     H
//
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