AFTA_CORGL
ID AFTA_CORGL Reviewed; 661 AA.
AC Q8NTW4; Q6M8G6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Galactan 5-O-arabinofuranosyltransferase {ECO:0000250|UniProtKB:P9WN03};
DE EC=2.4.2.46 {ECO:0000250|UniProtKB:P9WN03};
DE AltName: Full=Arabinofuranosyltransferase AftA {ECO:0000305|PubMed:16595677};
GN Name=aftA {ECO:0000303|PubMed:16595677}; OrderedLocusNames=Cgl0188, cg0236;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP FUNCTION IN ARABINAN BIOSYNTHESIS, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16595677; DOI=10.1074/jbc.m600045200;
RA Alderwick L.J., Seidel M., Sahm H., Besra G.S., Eggeling L.;
RT "Identification of a novel arabinofuranosyltransferase (AftA) involved in
RT cell wall arabinan biosynthesis in Mycobacterium tuberculosis.";
RL J. Biol. Chem. 281:15653-15661(2006).
CC -!- FUNCTION: Involved in the biosynthesis of the arabinogalactan (AG)
CC region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an
CC essential component of the cell wall (PubMed:16595677). Catalyzes the
CC addition of the first key arabinofuranosyl (Araf) residue from the
CC sugar donor decaprenyl-phospho-arabinose (DPA) on the C-5 of a 6-linked
CC galactofuranosyl (Galf) of the galactan domain, thus 'priming' the
CC galactan for further elaboration by other arabinofuranosyltransferases
CC (By similarity). {ECO:0000250|UniProtKB:P9WN03,
CC ECO:0000269|PubMed:16595677}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Adds an alpha-D-arabinofuranosyl group from trans,octacis-
CC decaprenylphospho-beta-D-arabinofuranose at the 5-O-position of the
CC eighth, tenth and twelfth galactofuranose unit of the galactofuranan
CC chain of [beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-
CC (1->6)]14-beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-
CC (1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-
CC diphospho-trans,octacis-decaprenol.; EC=2.4.2.46;
CC Evidence={ECO:0000250|UniProtKB:P9WN03};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:16595677}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have a cell wall that
CC shows a complete absence of arabinose resulting in a truncated cell
CC wall structure possessing only a galactan core with a concomitant loss
CC of cell wall-bound corynomycolic acids. {ECO:0000269|PubMed:16595677}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 85 family.
CC {ECO:0000305}.
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DR EMBL; BA000036; BAB97581.1; -; Genomic_DNA.
DR EMBL; BX927148; CAF18758.1; -; Genomic_DNA.
DR RefSeq; NP_599441.1; NC_003450.3.
DR AlphaFoldDB; Q8NTW4; -.
DR STRING; 196627.cg0236; -.
DR CAZy; GT85; Glycosyltransferase Family 85.
DR KEGG; cgb:cg0236; -.
DR KEGG; cgl:Cgl0188; -.
DR PATRIC; fig|196627.13.peg.192; -.
DR eggNOG; ENOG502ZB59; Bacteria.
DR HOGENOM; CLU_021304_0_0_11; -.
DR OMA; YPAGWFW; -.
DR BRENDA; 2.4.2.46; 960.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR020959; ArabinofuranosylTrfase_AftA_C.
DR InterPro; IPR020963; ArabinofuranosylTrfase_AftA_N.
DR Pfam; PF12249; AftA_C; 1.
DR Pfam; PF12250; AftA_N; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..661
FT /note="Galactan 5-O-arabinofuranosyltransferase"
FT /id="PRO_0000420576"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 661 AA; 72570 MW; B8F00CF82DE4EF65 CRC64;
MNPYGPSRVP EGEVYRPDRL NRKATLVAIV GAAILAFAFA LVLWMGLKQT NLPAFGPSNV
TRAVASATIA AVLIVTGFLT WLWLRDEHQS NPRWELEDVK PRPKWRTALT YLASYLSPAA
LVVAVLAIPL SATRLYLDGI SVDQGFRTQF LTRMADDIGL SDMNYIDMPT FYPAGWFWLG
GRLANLLGLP GWEAFQPWAI VSMAVAASVL VPVWQRITGS LPVATGIALV TTCIILAMNS
EEPYAAIVAM GIPAMLVLAS RIAKGDKFAL AGGIIYLGVS ATFYTLFTGA IALSAVAVCI
VVAAIVQRSI KPLLWLAVLG GGSIVIALIS WGPYLLASIN GAERSGDSAT HYLPLEGTQF
PVPFLASSVV GLLCLVGLIY LVVRFHNNEV RAMWVGIAVF YAWMGMSMAI TLLGNTLLGF
RLDTVLVLIF ATAGVLGIAD FRLASVYQLY PTQITERTAT HLTNLIVVLV LLGGLYYAQD
LPQKNARAID LAYTDTDGYG ERADLYPAGA ARYYKDINDH LLDQGFEPSE TVVLTDELDF
MSYYPYRGYQ AFTSHYANPL GEFGNRNAFI EDLAIRSWDE LADPQQFSDA LNTSPWTIPE
VFIFRGSIDD PDAGWKYDVA EDLYPNNPNV RFRGVYFNPE SFDQMWQTKQ VGPFVVVTHN
E
