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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//