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Database: UniProt
Entry: C7MPG0_CRYCD
LinkDB: C7MPG0_CRYCD
Original site: C7MPG0_CRYCD 
ID   C7MPG0_CRYCD            Unreviewed;       889 AA.
AC   C7MPG0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|HAMAP-Rule:MF_01395};
DE   Includes:
DE     RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE              Short=ACCase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE              Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE              EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_00823};
DE   Includes:
DE     RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE              Short=ACCase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE              Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
GN   Name=accD {ECO:0000256|HAMAP-Rule:MF_01395};
GN   Synonyms=accA {ECO:0000256|HAMAP-Rule:MF_00823};
GN   OrderedLocusNames=Ccur_11100 {ECO:0000313|EMBL:ACU94800.1};
OS   Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 /
OS   12-3).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Cryptobacterium.
OX   NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU94800.1, ECO:0000313|Proteomes:UP000000954};
RN   [1] {ECO:0000313|EMBL:ACU94800.1, ECO:0000313|Proteomes:UP000000954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700683 / DSM 15641 / 12-3
RC   {ECO:0000313|Proteomes:UP000000954};
RX   PubMed=21304644; DOI=10.40456/sigs.12260;
RA   Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA   Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P.,
RA   D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Cryptobacterium curtum type strain (12-3).";
RL   Stand. Genomic Sci. 1:93-100(2009).
CC   -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC       Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its
CC       carrier protein (BCCP) and then the CO(2) group is transferred by the
CC       transcarboxylase to acetyl-CoA to form malonyl-CoA.
CC       {ECO:0000256|ARBA:ARBA00025280, ECO:0000256|HAMAP-Rule:MF_01395}.
CC   -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC       First, biotin carboxylase catalyzes the carboxylation of biotin on its
CC       carrier protein (BCCP) and then the CO(2) group is transferred by the
CC       carboxyltransferase to acetyl-CoA to form malonyl-CoA.
CC       {ECO:0000256|HAMAP-Rule:MF_00823}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00823};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01395};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01395};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956,
CC       ECO:0000256|HAMAP-Rule:MF_00823}.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC       carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC       subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta
CC       (AccD). {ECO:0000256|HAMAP-Rule:MF_00823}.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterotetramer composed of biotin
CC       carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC       subunits of ACCase subunit beta/alpha. {ECO:0000256|ARBA:ARBA00011664}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00823}.
CC   -!- SIMILARITY: Belongs to the AccA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00823}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01395}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the AccA family.
CC       {ECO:0000256|ARBA:ARBA00006276}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AccD/PCCB family.
CC       {ECO:0000256|ARBA:ARBA00010284}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01395}.
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DR   EMBL; CP001682; ACU94800.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7MPG0; -.
DR   STRING; 469378.Ccur_11100; -.
DR   KEGG; ccu:Ccur_11100; -.
DR   eggNOG; COG0777; Bacteria.
DR   eggNOG; COG0825; Bacteria.
DR   HOGENOM; CLU_015486_4_1_11; -.
DR   OMA; MHVADEV; -.
DR   OrthoDB; 9772975at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000000954; Chromosome.
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-KW.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00823; AcetylCoA_CT_alpha; 1.
DR   HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   NCBIfam; TIGR00513; accA; 1.
DR   NCBIfam; NF041504; AccA_sub; 1.
DR   NCBIfam; TIGR00515; accD; 1.
DR   PANTHER; PTHR42853; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR42853:SF3; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR   Pfam; PF03255; ACCA; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01069; ACCCTRFRASEA.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00823}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00823};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW   Rule:MF_00823};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_00823};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00823};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00823}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00823}; Reference proteome {ECO:0000313|Proteomes:UP000000954};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00823}; Zinc {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}.
FT   DOMAIN          245..511
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          621..869
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          34..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ   SEQUENCE   889 AA;  95510 MW;  D9DEA587B65029D8 CRC64;
     MRVRAADKGS RKALTGPQKG GIVVEKEYYT YGSDETRDAK GIQATSSDQI ADETTTSTDT
     TSAVSYRLER IAEEALQKVL SGTDSSAAPN ATSAAALEEY TAVPSSARPH DDRTALVRAL
     VMSQGKNLRT LATAVCEAGM TPVTPFTDDR KPVPFSRIPG QTVRLGEHYG DALFSNAHAV
     LAAAEEASVQ VILLDGVSSA LSSVDSFLAR AQNRGIAVYR AIDSEHPLLG WQRCSTTRQL
     SEADEWVTCR HCGLTFDKKG VAKRHYTCPA CGGYFRMSSD ERINDLLDMG TFIEWDACLP
     ETDPLDFPGY EEKLTTQREK TGLQEAVRTG RGAIAGISLA IGVMEAGFFM GSMGSVVGEK
     VARLFDRATE AGLPVVVFTA SGGARMQEGL ISLMQMAKVS CAVERHAQAG LPYISVVTDP
     TTGGVTASFA TQADIILIEP RALLGFAGKR VIRDTIRQEL PEGFQTAEFA LEHGLVDAII
     ARDELRATLA HLLAVHLATQ SRPVREGSTE TIVNYQAVCR ALTSGHNTYN HVTYGRLPLT
     DAQPDEEGAL SSLIGMVKQV VQAHTDPVRT LRQTLEQGSY ETEDGSSLAM QSTVDEAESI
     SSDAAASESS HQADVAEAKP AANDALSSGS GNAWQSVQLA RNVHRPCSSY YINQIFDGFI
     ELHGDRSFAD DGAIIAGVGW LGNQAVTVIA QEKGADLKER IRRNFGCPQP EGYRKSLRLM
     RQAEKFNRPI VCLVDTQGAF CGADSEERGQ GNAIADNLVA MAGLRVPVVS VLCGEGGSGG
     ALALAVANKV GMQEHAVYSV LSPEGFASIL WKDRSRAPEA AEVMRMNANQ VYEMHVADEV
     VSEGSGPAHE NPEQAADNLR AFLTRSLAAL RNVSAEDLVR QRHERFAQY
//
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