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Database: UniProt
Entry: S0IV05_9FIRM
LinkDB: S0IV05_9FIRM
Original site: S0IV05_9FIRM 
ID   S0IV05_9FIRM            Unreviewed;       540 AA.
AC   S0IV05;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
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};
DE            EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_01395};
GN   Name=accD {ECO:0000256|HAMAP-Rule:MF_01395};
GN   ORFNames=C805_02586 {ECO:0000313|EMBL:EOT24374.1};
OS   Eubacterium sp. 14-2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1235790 {ECO:0000313|EMBL:EOT24374.1, ECO:0000313|Proteomes:UP000014176};
RN   [1] {ECO:0000313|EMBL:EOT24374.1, ECO:0000313|Proteomes:UP000014176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14-2 {ECO:0000313|EMBL:EOT24374.1,
RC   ECO:0000313|Proteomes:UP000014176};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Eubacterium bacterium 14-2.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- 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_01395};
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_01395}.
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_01395}.
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_01395}.
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: 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:EOT24374.1}.
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DR   EMBL; ASSS01000010; EOT24374.1; -; Genomic_DNA.
DR   RefSeq; WP_016215614.1; NZ_KE159568.1.
DR   AlphaFoldDB; S0IV05; -.
DR   STRING; 1235790.C805_02586; -.
DR   PATRIC; fig|1235790.3.peg.2788; -.
DR   eggNOG; COG0777; Bacteria.
DR   eggNOG; COG0825; Bacteria.
DR   HOGENOM; CLU_015486_3_2_9; -.
DR   OrthoDB; 9772975at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000014176; 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-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_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; NF041504; AccA_sub; 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; PR01070; ACCCTRFRASEB.
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_01395}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW   Rule:MF_01395};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_01395};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_01395};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_01395}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01395}; Reference proteome {ECO:0000313|Proteomes:UP000014176};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01395}; Zinc {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}.
FT   DOMAIN          5..271
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          266..520
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   ZN_FING         9..31
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ   SEQUENCE   540 AA;  61170 MW;  ADEFC5E07A23B809 CRC64;
     MQKTDYRICR ACNAKTDRKL LKENYFICPE CGGYLRFHAD ERIQSLADEE SFREWDQNLE
     LDVSGIEDAY AQKLAETSEK YNLKEAVITG EIKINGISAA IGVMDSRFLM ASMGYVVGEK
     VTRLFERATE KKLPVILFSC SGGARMQEGI ISLMQMSKTA AAVQKHSEEG LLYISVLTNP
     TMGGVTASFA MLADIIFAEK SAVVGFAGRR VIEQNVGDRL PDEFQTAEFQ VAHGFVDEVM
     LREETRDRLG LLLELHRKNG TARYRKWNIK PLTVRKNRTC LTPWEKVKYA RSADRPMSRD
     YIDRLFQVFV ELKGDRISGD DHAVVAGIAE FHGQAVTVIG QERGKKSLKD AVYRNWGMML
     PCGYRKVLRL MKQAEKFHRP VICFIDTIGA ACGREAEEAG QGTMIANLLE EAAAIKVPIL
     SVLIGEGYSG GALALAVANE VWMMENAVYS ILSPEGYASI LWKDNRRAKE AAREMKMEAD
     DLCRLQIVDK VIEEKEAVNS RNIDCVCRVL NREILQFMER YSNKSEKDIV DERYRRYRKY
//
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