ACCD4_MYCTU
ID ACCD4_MYCTU Reviewed; 522 AA.
AC O53578; F2GDF8; I6YH65; Q8VIT5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Biotin-dependent long chain acyl-coenzyme A carboxylase beta4 subunit {ECO:0000305};
DE EC=2.1.3.- {ECO:0000269|PubMed:16354663, ECO:0000269|PubMed:28222482};
GN Name=accD4 {ECO:0000303|PubMed:16354663};
GN OrderedLocusNames=Rv3799c {ECO:0000312|EMBL:CCP46628.1};
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 PROTEIN SEQUENCE OF 3-8, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
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 INDUCTION.
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 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: Component of a biotin-dependent acyl-CoA carboxylase complex.
CC This subunit transfers the CO2 from carboxybiotin to the CoA ester
CC substrate (PubMed:16354663, PubMed:28222482). When associated with the
CC alpha3 subunit AccA3, the beta5 subunit AccD5 and the epsilon subunit
CC AccE5, forms the LCC complex, which is involved in the carboxylation of
CC long chain acyl-CoA (PubMed:16354663, PubMed:28222482). The LCC complex
CC can use C16-C24 substrates, the highest specific activity is obtained
CC with carboxy-C20-CoA (PubMed:28222482). Has low activity with acetyl-
CC CoA and propionyl-CoA (PubMed:16354663). {ECO:0000269|PubMed:16354663,
CC ECO:0000269|PubMed:28222482}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=32 uM for carboxy-C20-CoA (in the presence of AccA3, AccD5 and
CC AccE5) {ECO:0000269|PubMed:28222482};
CC Vmax=2.44 nmol/min/mg enzyme with carboxy-C20-CoA as substrate (in
CC the presence of AccA3, AccD5 and AccE5)
CC {ECO:0000269|PubMed:28222482};
CC -!- SUBUNIT: The biotin-dependent long-chain acyl-CoA carboxylase (LCC)
CC complex is composed of AccA3, which contains the biotin carboxylase
CC (BC) and biotin carboxyl carrier protein (BCCP) domains, and AccD4,
CC which contains the carboxyl transferase (CT) domain (PubMed:16354663,
CC PubMed:28222482). The complex also contains the beta5 subunit AccD5 and
CC the epsilon subunit AccE5. The four subunits are essential for
CC activity, but AccD5, together with AccE5, probably plays a structural
CC role rather than a catalytic one (PubMed:28222482).
CC {ECO:0000269|PubMed:16354663, ECO:0000269|PubMed:28222482}.
CC -!- INDUCTION: Expressed at higher levels during the exponential growth
CC phase. {ECO:0000269|PubMed:17114269}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46628.1; -; Genomic_DNA.
DR RefSeq; NP_218316.2; NC_000962.3.
DR RefSeq; WP_003420767.1; NZ_NVQJ01000022.1.
DR AlphaFoldDB; O53578; -.
DR SMR; O53578; -.
DR STRING; 83332.Rv3799c; -.
DR PaxDb; O53578; -.
DR PRIDE; O53578; -.
DR GeneID; 886131; -.
DR KEGG; mtu:Rv3799c; -.
DR PATRIC; fig|83332.111.peg.4224; -.
DR TubercuList; Rv3799c; -.
DR eggNOG; COG4799; Bacteria.
DR OMA; DFIEGYN; -.
DR PhylomeDB; O53578; -.
DR BioCyc; MetaCyc:G185E-8095-MON; -.
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:0005886; C:plasma membrane; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015977; P:carbon fixation; IDA:MTBBASE.
DR GO; GO:0071769; P:mycolate cell wall layer assembly; IMP:MTBBASE.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Transferase.
FT CHAIN 1..522
FT /note="Biotin-dependent long chain acyl-coenzyme A
FT carboxylase beta4 subunit"
FT /id="PRO_0000452370"
FT DOMAIN 11..261
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 270..503
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ SEQUENCE 522 AA; 56680 MW; 8D3BFF09F2D6F7FA CRC64;
MTVTEPVLHT TAEKLAELRE RLELAKEPGG EKAAAKRDKK GIPSARARIY ELVDPGSFME
IGALCRTPGD PNALYGDGVV TGHGLINGRP VGVFSHDQTV FGGTVGEMFG RKVARLMEWC
AMVGCPIVGI NDSGGARIQD AVTSLAWYAE LGRRHELLSG LVPQISIILG KCAGGAVYSP
IQTDLVVAVR DQGYMFVTGP DVIKDVTGED VSLDELGGAD HQASYGNIHQ VVESEAAAYQ
YVRDFLSFLP SNCFDKPPVV NPGLEPEITG HDLELDSIVP DSDNMAYDMH EVLLRIFDDG
DFLDVAAQAG QAIITGYARV DGRTVGVVAN QPMHMSGAID NEASDKAARF IRFSDAFDIP
LVFVVDTPGF LPGVEQEKNG IIKRGGRFLY AVVEADVPKV TITIRKSYGG AYAVMGSKQL
TADLNFAWPT ARIAVIGADG AAQLLMKRFP DPNAPEAQAI RKSFVENYNL NMAIPWIAAE
RGFIDAVIDP HETRLLLRKS MHLLRDKQLW WRVGRKHGLI PV
