ID A7HWL7_PARL1 Unreviewed; 1091 AA.
AC A7HWL7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN OrderedLocusNames=Plav_2692 {ECO:0000313|EMBL:ABS64300.1};
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS64300.1, ECO:0000313|Proteomes:UP000006377};
RN [1] {ECO:0000313|EMBL:ABS64300.1, ECO:0000313|Proteomes:UP000006377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966
RC {ECO:0000313|Proteomes:UP000006377};
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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DR EMBL; CP000774; ABS64300.1; -; Genomic_DNA.
DR RefSeq; WP_012111615.1; NC_009719.1.
DR AlphaFoldDB; A7HWL7; -.
DR STRING; 402881.Plav_2692; -.
DR KEGG; pla:Plav_2692; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_009218_0_0_5; -.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000006377; 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:0046872; F:metal ion binding; IEA:InterPro.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
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; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR48095:SF5; BLL7292 PROTEIN; 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; 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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 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|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000006377}.
FT DOMAIN 1..453
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 118..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 478..556
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 573..843
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 836..1075
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1091 AA; 116852 MW; 7C30F9B7C7953F87 CRC64;
MKSLLIANRG EIAVRIARAG AELGLRTVGV YAEDDALSLH VRAADEALPL TGTGAAAYLD
IKQIVAEAKQ AGCDAIHPGY GFLSENAAFA EECAKEGIIF VGPSPEALRL FGDKAKARAL
AEKEGVPLFP GTNGATSLEE ARAFMEKVKA PIMLKALAGG GGRGMRAVTD IKELPEAYER
CRSEATAAFG SGDLYAEKLV RKARHIEIQI VGDGKDVIDL GERECTLQRR NQKVVEVAPS
PTLDAGLRKR LVEAARKLAG AANYKGLGTF EFLIDMEAKS AESAIAFMEA NPRLQVEHTV
TEEVTGVDLV KTQLRIAGGA TLKEVGLTET PSPRGFAIQL RVNMERMNET GEAVPTGGVL
NTFNPPSGPG IRVDTFGYAG YRTSPNYDSL LAKLIAHSPA PDYAAAVARA RRALSEFQIE
GVTTNISFLQ ALMARDDVQA NEVSTGFIAE HAGELAKAEA TPGRYFTGGN GTGAAAAARH
VEGPAGTTPV PSSMQGKVIS VDVAEGATVA KGQQIAVLEA MKMEHTIAAP FGGTVRKIAA
VTNATLMEGE PILFIEEGAG DDAAAVTEEA VDPDYIRPDL QHVIERHALG LDENRPDAVA
RRRKRNQRTV RENIDQLCDE GSFIEYGALA LAAQRRRRSL EELLKMSPAD GLVSGIGTVN
ASLFGEEKAR AMVMGYDFTV FAGTQGAMNH KKMDRMLFLA RDQKLPIVLL AEGGGGRPGD
TDTAGVAGLD TPSFHTFATL SGKVPLVGMT AGRCFAGNAA LLGCCDVIIA TADSNIGMGG
PAMIEGGGLG VYAPEDIGPA AVHRKNGVID IFVKDEEEAI EACQKYLSYF QGAVEKWEES
DQRLLRHMIP ENRLRAYDID KVIEGVADKG SVLELRREFG IGIKTALIRM EGRPMGLMAN
NPYHLGGAID AEAADKAARF MQLCDAFGLP ILSLCDTPGF MVGPEIEKEA QVRHVSRMFV
TAANMSVPLF AVVLRKGYGL GAQAMTAGSF HAPFFNISWP TGEFGGMGLE GAARLGYRRE
MEAIEDPEER DAFYRKMVDR YYENGKATNM AAFLEIDAVI DPAETRHWIT RGLKSLPPME
AKPSRAFIDT W
//
