ACCE5_MYCTU
ID ACCE5_MYCTU Reviewed; 177 AA.
AC P96886; I6YBP4; L0TEV5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase epsilon subunit {ECO:0000305};
GN Name=accE5 {ECO:0000303|PubMed:16385038};
GN OrderedLocusNames=Rv3281 {ECO:0000312|EMBL:CCP46100.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, SUBUNIT, INDUCTION, AND DOMAIN.
RX PubMed=16354663; DOI=10.1074/jbc.m511761200;
RA Oh T.J., Daniel J., Kim H.J., Sirakova T.D., Kolattukudy P.E.;
RT "Identification and characterization of Rv3281 as a novel subunit of a
RT biotin-dependent acyl-CoA carboxylase in Mycobacterium tuberculosis
RT H37Rv.";
RL J. Biol. Chem. 281:3899-3908(2006).
RN [3]
RP FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=16385038; DOI=10.1128/jb.188.2.477-486.2006;
RA Gago G., Kurth D., Diacovich L., Tsai S.C., Gramajo H.;
RT "Biochemical and structural characterization of an essential acyl coenzyme
RT A carboxylase from Mycobacterium tuberculosis.";
RL J. Bacteriol. 188:477-486(2006).
RN [4]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=17114269; DOI=10.1128/jb.01019-06;
RA Daniel J., Oh T.J., Lee C.M., Kolattukudy P.E.;
RT "AccD6, a member of the Fas II locus, is a functional carboxyltransferase
RT subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis.";
RL J. Bacteriol. 189:911-917(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=28222482; DOI=10.1111/febs.14046;
RA Bazet Lyonnet B., Diacovich L., Gago G., Spina L., Bardou F., Lemassu A.,
RA Quemard A., Gramajo H.;
RT "Functional reconstitution of the Mycobacterium tuberculosis long-chain
RT acyl-CoA carboxylase from multiple acyl-CoA subunits.";
RL FEBS J. 284:1110-1125(2017).
CC -!- FUNCTION: Stimulates activity of the AccA3/AccD5 biotin-dependent acyl-
CC CoA carboxylase complex (PubMed:16354663, PubMed:16385038). Interacts
CC with AccD5 and modulates its carboxylase activity for acetyl-CoA and
CC propionyl-CoA (PubMed:16354663, PubMed:16385038). Inhibits activity of
CC the AccA3/AccD6 complex (PubMed:17114269). Is also required for the
CC activity of the long-chain acyl-CoA carboxylase (LCC) complex
CC (PubMed:28222482). {ECO:0000269|PubMed:16354663,
CC ECO:0000269|PubMed:16385038, ECO:0000269|PubMed:17114269,
CC ECO:0000269|PubMed:28222482}.
CC -!- SUBUNIT: Interacts with the AccA3/AccD5 biotin-dependent acyl-CoA
CC carboxylase complex (PubMed:16354663, PubMed:16385038). Interacts with
CC the AccA3/AccD6 complex (PubMed:17114269). Is also part of the long-
CC chain acyl-CoA carboxylase (LCC) complex, which is composed of AccA3,
CC AccD4, AccD5 and AccE5. The four subunits are essential for activity,
CC but AccD5, together with AccE5, probably plays a structural role rather
CC than a catalytic one (PubMed:28222482). {ECO:0000269|PubMed:16354663,
CC ECO:0000269|PubMed:16385038, ECO:0000269|PubMed:17114269,
CC ECO:0000269|PubMed:28222482}.
CC -!- INDUCTION: Protein level is maximal in exponential growth phase and
CC declines during late log and stationary phase.
CC {ECO:0000269|PubMed:16354663}.
CC -!- DOMAIN: It is uncertain whether the five sets of tandem repeats at the
CC N terminus are required, or not, for maximal enhancement of carboxylase
CC activity. {ECO:0000305|PubMed:16354663, ECO:0000305|PubMed:16385038}.
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DR EMBL; AL123456; CCP46100.1; -; Genomic_DNA.
DR RefSeq; NP_217798.1; NC_000962.3.
DR RefSeq; WP_010886160.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; P96886; -.
DR STRING; 83332.Rv3281; -.
DR PaxDb; P96886; -.
DR PRIDE; P96886; -.
DR DNASU; 888732; -.
DR GeneID; 888732; -.
DR KEGG; mtu:Rv3281; -.
DR PATRIC; fig|83332.111.peg.3663; -.
DR TubercuList; Rv3281; -.
DR eggNOG; ENOG5031SCM; Bacteria.
DR OMA; THEPHIE; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:MTBBASE.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IDA:MTBBASE.
DR GO; GO:0015977; P:carbon fixation; IDA:MTBBASE.
DR InterPro; IPR032716; ACC_epsilon.
DR Pfam; PF13822; ACC_epsilon; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..177
FT /note="Biotin-dependent acetyl-/propionyl-coenzyme A
FT carboxylase epsilon subunit"
FT /id="PRO_0000452371"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 177 AA; 19014 MW; 7B618CA28EE9E428 CRC64;
MGTCPCESSE RNEPVSRVSG TNEVSDGNET NNPAEVSDGN ETNNPAEVSD GNETNNPAPV
SRVSGTNEVS DGNETNNPAP VSRVSGTNEV SDGNETNNPA PVTEKPLHPH EPHIEILRGQ
PTDQELAALI AVLGSISGST PPAQPEPTRW GLPVDQLRYP VFSWQRITLQ EMTHMRR
