ID B8ZQE1_MYCLB Unreviewed; 457 AA.
AC B8ZQE1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 32.
DE RecName: Full=Coenzyme F420:L-glutamate ligase;
DE EC=6.3.2.31;
DE EC=6.3.2.34;
DE AltName: Full=Coenzyme F420-0:L-glutamate ligase;
DE AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase;
GN Name=fbiB; OrderedLocusNames=MLBr00758;
OS Mycobacterium leprae (strain Br4923).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=561304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Br4923;
RX PubMed=19881526; DOI=10.1038/ng.477;
RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D.,
RA Paniz-Mondolfi A., Matsuoka M., Taylor G.M., Donoghue H.D.,
RA Bouwman A., Mays S., Watson C., Lockwood D., Khamispour A.,
RA Dowlati Y., Jianping S., Rea T.H., Vera-Cabrera L., Stefani M.M.,
RA Banu S., Macdonald M., Sapkota B.R., Spencer J.S., Thomas J.,
RA Harshman K., Singh P., Busso P., Gattiker A., Rougemont J.,
RA Brennan P.J., Cole S.T.;
RT "Comparative genomic and phylogeographic analysis of Mycobacterium
RT leprae.";
RL Nat. Genet. 41:1282-1289(2009).
CC -!- FUNCTION: Catalyzes the GTP-dependent successive addition of
CC multiple gamma-linked L-glutamates to the L-lactyl phosphodiester
CC of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form
CC polyglutamated F420 derivatives (By similarity).
CC -!- CATALYTIC ACTIVITY: GTP + coenzyme F420-0 + L-glutamate = GDP +
CC phosphate + coenzyme F420-1.
CC -!- CATALYTIC ACTIVITY: GTP + coenzyme F420-0 + n L-glutamate = GDP +
CC phosphate + coenzyme gamma-F420-n.
CC -!- CATALYTIC ACTIVITY: GTP + coenzyme F420-1 + L-glutamate = GDP +
CC phosphate + coenzyme gamma-F420-2.
CC -!- COFACTOR: Binds 2 divalent metal cations per subunit. The ions
CC could be magnesium and/or manganese (By similarity).
CC -!- COFACTOR: Monovalent cation. The ion could be potassium (By
CC similarity).
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CofE family.
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DR EMBL; FM211192; CAR70852.1; -; Genomic_DNA.
DR RefSeq; YP_002503218.1; NC_011896.1.
DR ProteinModelPortal; B8ZQE1; -.
DR STRING; 561304.MLBr_00758; -.
DR EnsemblBacteria; CAR70852; CAR70852; MLBr00758.
DR GeneID; 7326230; -.
DR KEGG; mlb:MLBr_00758; -.
DR PATRIC; 18042282; VBIMycLep121698_1372.
DR eggNOG; COG1478; -.
DR KO; K12234; -.
DR OMA; PAPHHTT; -.
DR ProtClustDB; PRK13294; -.
DR BioCyc; MLEP561304:GJP6-773-MONOMER; -.
DR UniPathway; UPA00071; -.
DR GO; GO:0043773; F:coenzyme F420-0 gamma-glutamyl ligase activity; IEA:InterPro.
DR GO; GO:0052618; F:coenzyme F420-0:L-glutamate ligase activity; IEA:HAMAP.
DR GO; GO:0052619; F:coenzyme F420-1:gamma-L-glutamate ligase activity; IEA:HAMAP.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009108; P:coenzyme biosynthetic process; IEA:HAMAP.
DR GO; GO:0052645; P:F420-0 metabolic process; IEA:HAMAP.
DR GO; GO:0055114; P:oxidation-reduction process; IEA:GOC.
DR Gene3D; 3.40.109.10; -; 1.
DR HAMAP; MF_01259; F420_ligase_CofE_2; 1; -.
DR InterPro; IPR002847; F420-0_gamma-glut_ligase-rel.
DR InterPro; IPR008225; F420-0_gamma-glutamyl_ligase.
DR InterPro; IPR019943; F420_FbiB_C.
DR InterPro; IPR023661; F420_ligase_CofE_2_bact.
DR InterPro; IPR000415; Nitroreductase-like.
DR Pfam; PF01996; F420_ligase; 1.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; Nitroreductase; 1.
DR TIGRFAMs; TIGR01916; F420_cofE; 1.
DR TIGRFAMs; TIGR03553; F420_FbiB_CTERM; 1.
PE 3: Inferred from homology;
KW Complete proteome; GTP-binding; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Potassium.
FT NP_BIND 29 32 GTP (By similarity).
FT REGION 1 253 F420-0:gamma-glutamyl ligase (By
FT similarity).
FT REGION 254 457 Unknown (By similarity).
FT METAL 118 118 Divalent metal cation 1 (By similarity).
FT METAL 159 159 Divalent metal cation 1 (By similarity).
FT METAL 160 160 Divalent metal cation 2 (By similarity).
FT BINDING 59 59 GTP (By similarity).
FT BINDING 64 64 GTP (By similarity).
FT BINDING 121 121 GTP (By similarity).
SQ SEQUENCE 457 AA; 48562 MW; 42BEF5D8A3333327 CRC64;
MTSSDSHRSA PSPEHGTAST IEILPVAGLP EFRPGDDLSA ALAAAAPWLR DGDVVVVTSK
VVSKCEGRLV PAPEDTRGRN ELRRKLINDE TIRVLARKGR TLIIENGLGL VQAAAGVDGS
NVGRGELALL PVNPDASAAV LRIGLRAMLG VNVAVVITDT MGRAWRNGQT DVAIGAAGLA
VLHNYSGAVD RYGNELVVTE IAVADEVAAA TDLVKGKLTA MPVAVVRGLS PTDDGSTAQH
LLRNGPDDLF WLGTTEALEL GRQQAQLLRR SVRQFSDEPI AAELIETAVA EALTAPAPHH
TRPVRFVWLQ TPAVRTRLLD RMADKWRLDL ASDALPADAI AQRVARGQIL YDAPEVIIPF
MVPDGAHAYP DAARASAEHT MFIVAVGAAV QALLVALAVR GLGSCWIGST IFADDLVRAE
LELPADWEPL GAIAIGYAHE PTDLREPVRV ADLLLRK
//
