(data stored in ACNUC7421 zone)

SWISSPROT: Q47T70_THEFY

ID   Q47T70_THEFY            Unreviewed;       501 AA.
AC   Q47T70;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 111.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   OrderedLocusNames=Tfu_0309 {ECO:0000313|EMBL:AAZ54347.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54347.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC       adenosylcobyrinic A,C-diamide. NH(2) groups are provided by
CC       glutamine, and one molecule of ATP is hydrogenolyzed for each
CC       amidation. {ECO:0000256|HAMAP-Rule:MF_00028,
CC       ECO:0000256|SAAS:SAAS00709802}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00028, ECO:0000256|SAAS:SAAS00709784}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00028, ECO:0000256|SAAS:SAAS00709810}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00028}.
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DR   EMBL; CP000088; AAZ54347.1; -; Genomic_DNA.
DR   RefSeq; WP_011290756.1; NC_007333.1.
DR   STRING; 269800.Tfu_0309; -.
DR   EnsemblBacteria; AAZ54347; AAZ54347; Tfu_0309.
DR   KEGG; tfu:Tfu_0309; -.
DR   eggNOG; ENOG4105CAA; Bacteria.
DR   eggNOG; COG1492; LUCA.
DR   HOGENOM; HOG000224803; -.
DR   KO; K02232; -.
DR   OMA; QVIIHGR; -.
DR   OrthoDB; 744477at2; -.
DR   BioCyc; TFUS269800:G1G4Q-311-MONOMER; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0015420; F:cobalamin-transporting ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00028; CobQ; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017929; CobB/CobQ_GATase.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR033949; CobQ_GATase1.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00313; cobQ; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47T70.
DR   SWISS-2DPAGE; Q47T70.
KW   Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00028,
KW   ECO:0000256|PROSITE-ProRule:PRU00606, ECO:0000256|SAAS:SAAS00709774};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00028,
KW   ECO:0000256|PROSITE-ProRule:PRU00606, ECO:0000256|SAAS:SAAS00056751};
KW   Ligase {ECO:0000313|EMBL:AAZ54347.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN      258    434       GATase cobBQ-type. {ECO:0000259|PROSITE:
FT                                PS51274}.
FT   ACT_SITE    426    426       {ECO:0000256|HAMAP-Rule:MF_00028}.
SQ   SEQUENCE   501 AA;  52815 MW;  7378F5D7BB92E313 CRC64;
     MSKAQGLLVA GTSSDAGKSL VTSALCRALA RHGIKVAPFK AQNMSNNSMV VPGPDGTGAE
     ISRAQWVQAL AARAEPETAM NPVLLKPSSD RGSHVVLRGR PFGRLAAGEF AGTRAVLAEA
     AYAALAELRS RYDVVVCEGA GGVAEINLRA HDYINMGLAR AADLPVIVIG DINRGGVFAS
     LYGSLALLDP ADQALVAGFV INKFRGDPSL LDPALKTLED LTGRPVLGVL PWQQNLWLES
     EDSLALTARE DGSAGTPVLR VAVVRLPRIG NTTDVDALGV EPGLRVDFVT SPRLLASADI
     VVLPDTRAVL TDLEWLRSRG LADAIANHAR HGGTVLGIGG GFQMLGRTIV DAEGVEGPAG
     RTVAGLSLLD LETVFTRNQT LNYSSGTWQG IPVGGYQSHY SRIQTGDGEA FPGGLRNGSV
     FGTMWHGSLE HDAFRGAWLA AAAENAGYDG SEYGQVCFAE VRDAYLDRLG DLAEEHLDMD
     AVLRLITEGA PKLPTVRGEL R
//

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